Studies on the β-form of isotactic polypropylene, 2. The melting behavior of predominantly β-form samples

Effects of crystallization conditions, heating rate, and isothermal annealing on the melting behavior of isotactic polypropylene samples with predominantly β-form were studied by differential scanning calorimetry. The results show that the β-form of these samples has a higher thermal stability and a lower recrystallization ability to the α-form after melting than the β-form of other samples.     

Functional β1 - and β2-adrenoceptors in the human myocardium

Functional β-adrenoceptor populations in the human heart were studied in vitro in electrically-paced strips of the right auricular and ventricular myocardium. The relative potency of selected agonists in producing inotropic responses (T_max, T′_max) in the presence of blockers for neuronal and extraneuronal uptakes was found to be as follows: isoprenaline > noradrenaline = adrenaline = salbutamol > dobutamine. Prenalterol had a negative inotropic effect in these preparations. The selective β₁ -(practoloI) and β₂-(H 35/25) blockers reduced inotropic responses to adrenaline (T_max, T′_max) and noradrenaline (T′_max) in the auricular strips. These results indicate the participation of β₂-adrenoceptors in inotropic responses in the human auricular and ventricular myocardium. For comparison, inotropic responses of electrically-paced rat myocardium to β-adrenergic agonists in the presence of blockers for neuronal and extraneuronal uptakes were likewise studied. The relative potencies for T_max were: noradrenaline = adrenaline > prenalterol > dobutamine = salbutamol. Given the high relative potency of salbutamol in the human myocardial strips (analogous to that previous shown in the β₂-dominated atria of the frog and trout) and the low relative potency of salbutamol in the rat tissue, these findings indicate a greater population of functionally active β₂-adrenoceptors in the human than in the rat myocardium.     

Cathepsin X cleaves the β2 cytoplasmic tail of LFA‐1 inducing the intermediate affinity form of LFA‐1 and α‐actinin‐1 binding

The motility of T cells depends on the dynamic spatial regulation of integrin‐mediated adhesion and de‐adhesion. Cathepsin X, a cysteine protease, has been shown to regulate T‐cell migration by interaction with lymphocyte function associated antigen‐1 (LFA‐1). LFA‐1 adhesion to the ICAM‐1 is controlled by the association of actin‐binding proteins with the cytoplasmic tail of the β₂ chain of LFA‐1. Cleavage by cathepsin X of the amino acid residues S⁷⁶⁹, E⁷⁶⁸ and A⁷⁶⁷ from the C‐terminal of the β₂ cytoplasmic tail of LFA‐1 is shown to promote binding of the actin‐binding protein α‐actinin‐1. Furthermore, cathepsin X overexpression reduced LFA‐1 clustering and induced an intermediate affinity LFA‐1 conformation that is known to associate with α‐actinin‐1. Increased levels of intermediate affinity LFA‐1 resulted in augmented cell spreading due to reduced attachment of T cells to the ICAM‐1‐coated surface. Gradual cleavage of LFA‐1 by cathepsin X enables the transition between intermediate and high affinity LFA‐1, an event that is crucial for effective T‐cell migration.     

Plastic deformation and solid-phase transformation in β-phase polypropylene

Tensile specimens of isotactic polypropylene, initially crystallized in the β-form with high purity, were tested at various temperatures. It was observed by WAXD that the most important phenomenon occurring in the course of a tensile test is the β-smectic transformation for specimens drawn at lower temperature and β-α transformation for specimens drawn at higher temperature, which takes place in the crystalline lamellae and is induced by plastic deformation. c-Axis oriented β-crystals have never been found in the drawn specimens. It was also shown that the β-smectic transformation propagates inside the spherulites from the equatorial regions, in which the chain axes are nearly parallel to the drawing direction, towards the diagonal and polar regions. Finally, it was noted that microvoids are formed simultaneously during plastic deformation, which may be due to the volume contraction induced by the β-α or β-smectic transformation.     

Distribution of α4β7 and αEβ7 integrins on thymocytes,intestinal epithelial lymphocytes and peripheral lymphocytes

β₇ is expressed on subsets of thymocytes, while T and B lymphocytes show heterogeneous expression of β₇. Here, we examine the phenotype of the thymocyte and lymphocyte subsets which express α₄β₇ and α_Eβ₇ using mAb against α_Eβ₇ and mAb DATK32 which recognizes a combinatorial epitope on α₄β₇. β₇⁺ thymocytes have a mature phenotype: TcR⁺, CD11a^hi CD44^hi HSA^dull. Small subsets of double-negative CD4_?CD8_?, single-positive CD4⁺ and CD8⁺ thymocytes express α₇, while double-positive CD4⁺ CD8⁺ thymocytes are β₇. However, two integrins α_Eβ₇ and α₄β₇ recognized by anti-β₇ are not expressed on an identical subpopulation of thymocytes, as β_Eα₇⁺α₄β₇^?, α_Eβ₇⁺α₄β₇⁺ and α_Eβ₇^?α₄β₇⁺ thymocyte subsets are evident. Similarly, intraepithelial lymphocytes express high levels of α_Eβ₇ but little α₄β₇. In the spleen, Peyer's patches and lymph nodes, α₄β₇ is expressed at higher levels on most B lymphocytes than on the majority of T lymphocytes, while a small subset of T lymphocytes, which includes both CD4⁺ and CD8⁺ lymphocytes, express high levels of β₇ in the form of α₄β₇ and α_Eβ₇, although, as observed with lymphocytes, not all α₄β₇^hi CD4^? lymphocytes expressed α₄β₇. The population of α₄β₇^hi CD4 lymphocytes are enriched in Peyer's patches and form subsets of the memory CD4⁺ lymphocyte population, which can be further subdivided on the basis of α_Eβ₇, L-selectin and α₄ expression. Therefore, memory CD4⁺ lymphocytes are highly heterogeneous in their expression of adhesion receptors, and presumably these subpopulations will exhibit very different trafficking properties.     

Synthesis and ring-opening polymerization of α-chloromethyl-α-methyl-β-propiolactone

α-Chloromethyl-α-methyl-β-propiolactone (CMMPL) was synthesized by dehydrohalogenation of α,α-dichloromethyl-β-propionic acid which was obtained by chlorination of α,α-hydroxymethyl-β-propionic acid (DMPA). Due to high strain of the four-numbered ring, CMMPL can be polymerized by ring-opening with or without an initiator. Both electrophiles like trifluoroacetic acid (TFAA) and nucleophiles like triethylamine (TEA) and pyridine, as well as organometallic compounds such as stannous octoate [Sn(Oct)₂)], aluminium triisopropoxide [Al(OⁱPr)₃] and tetrabutyl orthotitanate [Ti(OC₄H₉)₄], were found to be effective initiators. The polymerization can be conducted by either solution or bulk polymerization. P(CMMPL) is insoluble in almost all organic solvents at room temperature. An endothermic peak (ca. 214 ˜ 250°C) attributed to the melting transition of P(CMMPL) was observed in DSC curves. P(CMMPL) tends to have high crystallinity (40% ˜ 60%) as demonstrated by its X-ray diffraction patterns, and the crystallinity was found to vary with the types of initiator used.     

Copolymerization of γ-butyrolactone and β-butyrolactone

The copolymerization of a 4-membered β-butyrolactone (βBL) and a thermodynamically stable 5-membered γ-butyrolactone (γBL) proceeds in the bulk state with BF₃ · OEt₂ as a catalyst at room temperature to give poly[(3-hydroxybutyrate)-co-(4-hydroxybutyrate)] (P(3HB-co-4HB)) whose structure is identical with that of a polyester formed by microorganisms. The copolymer structure was confirmed by ¹H and ¹³C NMR spectroscopy. The monomer reactivity ratios were r_(γBL) = 0.48 and r_(βBL) = 0.58, respectively, and the unit composition of 4HB increases to 56% at high γBL to βBL ratio in the feed. End group analysis of the copolymer suggests the presence of a hydroxyl group and a carboxyl group at the ends of each polymer molecule. It was postulated that the monomers activated by BF₃ react with the hydroxy group derived from the water contaminant in the monomers.     

αEβ7 and α4β7 integrins associated with intraepithelial and mucosal homing,are expressed on macrophages

The two β₇ integrins α_Eβ₇ and α₄β₇ are the most recently described members of the integrins participating in intercellular binding. Their expression has been shown to be restricted to leukocytes and they have been suggested to be predominantly found in lymphocytes associating with the epithelium. Expression of β₇ has mainly been studied on lymphocytes whereas macrophages have been reported not to express the β₇ integrins. In this paper we have studied the expression of β₇ integrins in monocytoid cells. The myelomonocytic cell lines HL-60 and THP-1 did not express β₇ mRNA or protein, but differentiation of these cell lines to macrophages with phorbol 12-myristate 13-acetate (PMA) led to a strong induction of the β₇ mRNA expression. A clear but less pronounced up-regulation of β₇ mRNA-expression was also seen after treatment of HL-60 and THP-1 cells with interferon-γ (IFN-γ). However, its up-regulating effect on the surface expression of α₄β₇ and α_E7 complexes (detected by the monoclonal antibodies Act I and HML-1, respectively) exceeded that observed with PMA. To verify the in vitro cell line observations with normal cells, we also studied peripheral blood monocytes and tissue macrophages. Peripheral blood monocytes were Act I^? and HML-1^? in flow cytometry, but their expression was increased after a 72-h culture in the presence of PMA or IFN-γ. Also, several Act I⁺ and HML-1⁺ macrophages were found in immunohistochemical stainings of both liver and edemic lung biopsies as well as in lymph node sinuses. We therefore conclude that while monocytes do not express β₇ integrins the more differentiated cells of the monocyte-macrophage lineage do express both the α₄β₇ and α_Eβ₇ integrins, which might play a role in their intraepithelial homing.     

Induction and functional characterization of β 2-microglobulin (β2-μ)-free HLA class I heavy chains expressed by β2-μ-deficient human FO-1 melanoma cells

The frequent loss of β2-microglobulin (β₂-μ) in malignant cells has stimulated interest in the functional characteristics of β₂-μ-free HLA class I heavy chains, since this information contributes to assess the impact of β₂-μ abnormalities on the interaction of malignant cells with immune cells. Therefore, the present study has investigated the ability of β₂-μ-free HLA class I heavy chains to modulate NK cell-mediated lysis of melanoma cells and to present melanoma-associated antigen (MAA)-derived peptides to HLA class I-restricted, MAA-specific cytotoxic T lymphocytes (CTL). β₂-μ-free HLA class I heavy chains were induced on B₂m null FO-1 cells by sequential incubation with IFN-α for 48 h at 37 °C and for 24 h at 26 °C. Transfection of cells with a wild-type H-2L^d gene (FO-1L^d) enhanced the induction of β₂-μ-free HLA class I heavy chains under such experimental conditions. β₂-μ-free HLA class I heavy chains expressed on the cell membrane did not protect the B₂m null FO-1 cells from NK cell-mediated lysis. Furthermore, FO-1 cells which express β₂-μ-free HLA-A2 heavy chains following transfection with a wild-type HLA-A2 gene were not lysed by HLA-A2-restricted, MAA-specific CTL lines and clones. These results indicate that association with β₂-μ is required for interaction of HLA class I molecules with NK inhibitory receptors and for peptide presentation to CTL.     

Fluorescence study on intermolecular complex formation between mesogenic 4,4′-biphenyldicarboxylate moieties of thermotropic liquid-crystalline polyesters with 5 and 6 methylene units

The change in intermolecular complex formation between mesogenic 4,4′-biphenyldicarboxylate moieties of thermotropic liquid-crystalline (LC) polyesters containing 5 and 6 methylene units (BB-n, n = 5, 6) was studied by fluorescence technique. BB-5 shows a crystalline, an S_CA, and an isotropic phase during heating. BB-6 shows a crystalline mixture of β- and γ-phase, a pure γ-phase, an S_A, and an isotropic phase during heating. The fluorescence of BB-n is confirmed to be due to the formation of an intermolecular ground-state complex between two mesogenic 4,4′-biphenyldicarboxylate moieties, and shows a wavelength shift of the fluorescence peak to lower wavelengths upon heating. This is because the increase in thermal fluctuation with increasing temperature induces a decrease in interaction between two 4,4′-biphenyldicarboxylate moieties. Because of the constancy of the fluorescence peak wavelength in the LC phase of BB-n, LC phases for S_CA and S_A type molecular arrangements of the LC polyester with mesogenic biphenyl moieties were proved to show fluorescence around 376 and 360 nm, respectively. However, the shift of the fluorescence peak wavelength to lower wavelengths upon heating has been observed for the first time in the present study. The change in molecular interaction between the mesogenic moieties of the LCPs during heating is shown to result in various fluorescence patterns.     

Differential β3 and β1 Integrin Expression in Bone Marrow and Cortical Bone of Estrogen Deficient Rats

Integrin‐based (β₃) attachments to the extracellular matrix (ECM) on osteocyte cell processes have recently been proposed to play an important role in facilitating osteocyte mechanosensation. However, it is not yet known whether integrin expression is altered in the mechanoregulatory osteocytes during osteoporosis. The objective of this study was to test the hypothesis that the expression of integrin‐based mechanosensory complexes (β₁ and β₃ integrins) is altered as a direct response to estrogen deficiency, in an estrogen deficient animal model of osteoporosis. Four weeks post‐operatively, immunohistochemistry was used to detect for β₁ and β₃ integrin subunits in bone tissue and marrow of ovariectomized (OVX; N = 4) and SHAM (N = 4) operated animals. A tartrate resistant acid phosphatase (TRAP) control stain was performed to quantify the presence of osteoclasts in the bone marrow and bone surfaces. Image analysis was performed to quantify expression patterns in different biological compartments, that is, bone marrow, endosteum, and cortical bone. Our results showed that β₁ integrins were ubiquitously expressed throughout the bone and marrow, for both OVX and SHAM groups. β₃ integrin subunit expression was lower in bone cells from osteoporotic animals compared to controls, whereas β₃ expression in marrow cells did not differ significantly between groups. At the endosteum no difference was observed in β₃ integrin subunit expression. As expected, the number of osteoclasts was higher in the OVX group validating an imbalance in bone remodeling. We propose that a reduction in β₃ integrin expression in osteocytes might impair mechanosensation by bone cells during estrogen deficiency. Anat Rec, 298:1548–1559, 2015. © 2015 Wiley Periodicals, Inc.     

Coordinate expression of β1 and β2 integrin “activation” epitopes during T cell responses in secondary lymphoid tissue

The monoclonal antibodies (mAb) 15/7 and 24 recognize unique activation-dependent, conformational epitopes on β1 and β 2-integrins, respectively. The expression of both of these epitopes closely correlates with the ligand binding ability of their respective integrins, and thus serves as indicators of functional integrin “activation”. Here, we have used six-parameter flow cytometry to examine the expression of these epitopes and conventional β1- and β2-integrin epitopes during human T cell activation in secondary lymphoid tissues in vivo, focusing particularly on the virgin to memory/effector cell transition. Fresh tonsil lymphocytes were stained with mAb against conventional or activation-dependent integrin epitopes, followed by staining with mAb against CD3, CD45RA, and CD45RO, thus allowing the determination of integrin epitope expression on virgin (CD3⁺) T cells (CD45RA⁺/RO^?to±), memory/effector (CD45RA^?/RO⁺⁺) T cells, and T cells undergoing the virgin to memory/effector transition: transition region-1 (T1; CD45RA^+to++/RO⁺); -2 (T2; CD45RA⁺⁺/RO⁺⁺); and -3 (T3; CD45RA⁺/RO⁺⁺). Conventional β1- and β2-integrin epitopes progressively increase during the virgin to T3 stages of the transition in tonsil, in keeping with the generally higher levels of these adhesion molecules on memory/effector vs. virgin T cells. Expression of both the β1 (15/7)-and β2 (24)-integrin activation epitopes first appears on transitional T cells, and is maintained on a relatively constant number of cells (averaging 25-30%) throughout the T1-T3 stages. These epitopes are also noted on a subset of activated memory/effector T cells. Importantly, on both transitional and activated memory/effector T cell subsets, the expression patterns of the 15/7 and 24 epitopes vs. a variety of T cell activation antigens are identical, and the expression of these epitopes relative to each other is linearly correlated, findings strongly supporting the coordinate activation of β1 and β2 integrins duringT cell activation in vivo. These results provide the first evidence of integrin activation during an in vivo immunologic response, and demonstrate the usefulness of mAb recognizing conformational epitopes and multiparameter flow cytometry in delineating the dynamic interplay of adhesion molecules during complex physiologic processes.     

Kinetic determination of stereoselectivity in the anionic polymerization of α-ethyl-α-phenyl-β-propiolactone

The kinetics of the anionic polymerization of optically active α-ethyl-α-phenyl-β-propiolactone (optical purity 16,8%) initiated with bis(triphenylphosphine)iminium acetate was investigated and the rate constants for the homo-(k_ph) and crosspropagation (k_pc) (considering R and S enantiomers as comonomers) were determined. The knowledge of the values of k_ph and k_pc, equal to 1,53·10^?4 and 9,0·10^?51· mol^?1·s^?1, respectively (25°C, CH₂Cl₂ solvent), allowed us to calculate the distribution of homosequences in the polymer prepared from racemic monomer. The concentration of homosequences was slightly higher than calculated for the process with random enchainment of enantiomers. Thus, the content of homodyads, homotriads, and homotetrads equals 63, 40, and 25%, whereas for the random process it was 50, 25, and 13%, respectively. This difference is, however, too small to create homoblocks which could be responsible for the observed crystallinity of these polymers.     

Recognition of E-cadherin on epithelial cells by the mucosal T cell integrin αM290β7 (αEβ7)

The integrin α_M290β7 on the surface of a T cell hybridoma, MTC-1, mediated adhesion of these cells to the mouse epithelial cell line CMT93. This interaction was critically dependent on the presence of divalent cations; Mn²⁺ strongly promoted adhesion, Ca²⁺ was ineffective and Mg²⁺ gave intermediate results. Antibodies to molecules on the surface of CMT93 cells were tested for inhibition of adhesion. One monoclonal antibody (mAb) against E-cadherin, ECCD-2, was found to have significant inhibitory activity. Other mAb to E-cadherin and antibodies to other molecules had no effect. To show that inhibition by ECCD-2 was specific for adhesion mediated by α_M290β7, MTC-1 cells were induced to adhere to CMT93 via the LFA-1/ICAM-1 pathway. For this purpose, the epithelial cells were treated with interferon-γ and tumor necrosis factor-α to induce ICAM-1 expression and, in addition, α_M290β7 on MTC-1 cells was down-regulated by culturing the cells in the absence of transforming growth factor β. Under these circumstances adhesion of MTC-1 cells to CMT93 was inhibited by an antibody to LFA-1 but not by ECCD-2. Transfection of mouse L cells with cDNA for mouse E-cadherin enabled MTC-1 cells to adhere to them through the α_M290β7 integrin; this interaction was inhibited both by ECCD-2 and by blocking antibody against the integrin. These data strongly suggest that E-cadherin is a principal ligand for α_M290β7.     

Polylactones, 29. Preferentially syndiotactic poly(β-(R,S)-butyrolactone) obtained by ring-opening polymerization with triphenyltin methoxide or diphenyltin dimethoxide

Triphenyltin methoxide (Ph₃SnOMe) and diphenyltin dimethoxide (Ph₂Sn(OMe)₂)-initiated polymerizations of β-(R,S)-butyrolactone were conducted in bulk at 50 and 75°C. The low catalytic reactivity of the initiator prevented lower temperatures. The stereosequences of the isolated poly(β-(R,S)-butyrolactones) were analyzed by ¹³C NMR spectroscopy and characterized by the ratio of isotactic and syndiotactic diads (i/s-ratios down to 0,4/1,0 were found). With Ph₃SnOMe relatively high molecular weights (η_inh = 0,3 dL/g, M?_w ≈ 25 000?30000) were obtained but the stereoselectivity of the polymers obtained with both Ph₃SnOMe and Ph₂Sn(OMe)₂ is not higher than that with Bu₃SnOMe (published previously). Selected poly(β-(R,S)-butyrolactone) samples were characterized by IR spectra, WAXS powder patterns and DSC measurements.     

MAdCAM-1 costimulates T cell proliferation exclusively through integrin α4β7, whereas VCAM-1 and CS-1 peptide use α4β1: evidence for “remote” costimulation and induction of hyperresponsiveness to B7 molecules

We have analyzed the effects of the α⁴ integrin ligands mucosal addressin cell adhesion molecule-1 (MAdCAM-1), vascular cell adhesion molecule-1 (VCAM-1), and the fibronectin CS-1 splice variant on T cell activation. Immobilized MAdCAM-1 and VCAM-1 IgG-Fc chimeras and a fibronectin CS-1 peptide efficiently costimulate T cell proliferation when antigen presentation is mimicked by anti-CD3 antibody. VCAM-1-Fc and fibronectin CS-1, which are adhesive ligands for both the α⁴ β₁ and α⁴ β₇ integrins, medicate T cell costimulation exclusively through integrin α⁴ β₁, but not through α⁴ β₇. The inability of VCAM-1-Fc to costimulate via α⁴ β₇ suggests that cell adhesion per se is insufficient, and that exquisite recognition and activation events must be triggered. MAdCAM-1-Fc mediates costimulation exclusively via α⁴ β₇, and can both synergize with and induce hyperresponsiveness to the classical costimulator B7-2. MAdCAM-1-Fc and VCAM-1-Fc, but not B7-2, effectively costimulate when immobilized on sites spatially distant from the anti-CD3 antibody (“remote” costimulation). In vitro, the relative potencies of the CAM were VCAM-1-Fc > ICAM-1-Fc > MAdCAM-1-Fc > B7-Fc, except at high concentrations where ICAM-1 was the most potent. Features of costimulatory CAM revealed by this study have important implications for the design of immunotherapeutic vaccine strategies to combat cancer and infection.     

Developmental expression of the αIELβ7 integrin on T cell receptor γδ and T cell receptor αβ T cells

A novel monoclonal antibody, 2E7, was shown by immunoprecipitation to be reactive with the α_IELβ7 integrin and was employed to analyze the expression of this integrin in lymphocyte subsets and during T cell ontogeny. In adult lymph nodes, α_IEL was expressed at low levels by 40–70% of CD8⁺ T cells and < 5% of CD4⁺ T cells. However, virtually all intestinal intraepithelial lymphocytes and ?20% of lamina propria CD4⁺ T cells were 2E7⁺, indicating a preferential expression of this integrin on mucosal T cells. Examination of α_IEL integrin expression during thymus ontogeny revealed that ?3–5% of fetal or adult thymocytes were 2E7⁺. Interestingly, early in fetal thymus ontogeny, ?40% of 2E7⁺ cells expressed T cell receptor (TcR)-γδ and this subset persisted through birth. A developmental switch occurred such that 2E7⁺ TcR^? CD4^?8⁺ cells detected on fetal day 19 were followed by 2E7⁺ TcR-αβ CD4^?8⁺ cells in the neonatal thymus. The latter population persisted throughout thymus ontogeny into adulthood. Interestingly, a subset of TcR-γδ Vγ3⁺ day 16 fetal thymocyte dendritic epidermal cell (DEC) precursors were 2E7⁺, but all mature DEC expressed high levels of α_IEL integrin, suggesting that the α_IEL integrin was acquired late in DEC maturation. This possibility was strenghthened by immunohistochemical localization of the majority of 2E7⁺ γδ and αβ T cells to the medullary regions of the thymus. Overall, the results demonstrate a developmentally ordered expression pattern of the α_IELβ₇ integrin that suggests a common function for this integrin during TcR-γδ and -αβ CD4^?8⁺ T cell thymocyte development or perhaps in effector functions for these subsets.     

Expression of functionally active α4β1 integrin by thymic epithelial cells

We have investigated the expression and function of the VLA-4 heterodimer α₄β₁, a member of the β₁ integrin subfamily, on human thymic epithelial cells (TEC) derived from cortical epithelium. The expression of the α₄ integrin chain was studied in four different cloned TEC lines derived from either fetal or post-natal human thymus by both flow cytometry and immunoprecipitation techniques with anti-α₄ MoAbs. All different cell lines assayed expressed significant levels of α₄, as revealed by their reactivity with MoAbs specific for distinct α₄ epitopes. The α₄ subunit expressed by TEC was associated to β₁ but not to β₇ chain, and displayed the characteristic 80/70 kD pattern of proteolytic cleavage. The VLA-4 integrin in these cells was constitutively active in terms of adhesiveness to both fibronectin and vascular cell adhesion molecule-1 (VCAM-1). In addition, this heterodimer localized to punctate regions of the cell in the area of contact with the substratum, named point contacts assessed by staining with the anti-β₁ activation epitope 15/7 MoAb. According to the cortical origin of the TEC lines expressing VLA-4, human thymus sections stained with different anti-α₄ antibodies revealed the presence of cortical, and in smaller numbers medullary epithelial cells bearing α₄ integrin. The expression of α₄ in the thymus was also found in both adult and fetal rats, in which epithelial cells were also specifically stained. Altogether, our data show that VLA-4 is an additional component of the integrin repertoire of TEC, and suggest that it could have an important role in thymus epithelial cell–thymocyte interactions.     

Classification of β-adrenoceptors in the microcirculation of skeletal muscle

Nervous and humoral β-adrenergic, postjunctional effects on microvascular resistance, on precapillary sphincter tone, and on transcapillary fluid exchange in cat skeletal muscle (Lundvall & Järhult 1974, 1976 a, Lundvall & Hillman 1978 a, b) were evaluated with regard to the β₁-or β₂,-specificity of the adrenoceptors. Marked β₂-dilator responses but no significant β₁-effects were observed. The conclusion was therefore reached that neurogenic as well as humoral β-adrenergic control of the microcirculation in skeletal muscle is exerted via activation of β₂-adrenoceptors.