Primary localized cutaneous nodular amyloidosis successfully treated with cyclophosphamide

Primary localized cutaneous nodular amyloidosis (PLCNA) is a rare subtype of localized cutaneous amyloidosis and can be associated with various connective tissue disorders. It can be difficult to treat and past therapies include surgical excision, dermabrasion, electrodessication and curettage, cryotherapy and laser therapy. We present a case of a middle‐aged woman with PLCNA associated with CREST (calcinosis, Raynaud phenomenon, oesophageal motility disorders, sclerodactyly and telangiectasia) syndrome and Sjögren's syndrome responding to cyclophosphamide with no new amyloid deposits and resolution of skin ulceration after many years of resistance to drug therapy. It is important to monitor these patients for progression into systemic amyloidosis.     

Primary localized cutaneous nodular amyloidosis in a patient with Sjögren's syndrome: a review of the literature

We report a 53‐year‐old Japanese woman with multiple, red, and elastic soft nodules on the left waist, left thigh, and right lower leg. She had had polyclonal hyperglobulinemia for one year, rheumatoid arthritis for 13 years, and Sjögren's syndrome (SjS) for 18 years. Histochemical examination of the nodule on the left thigh revealed a deposition of amyloid by Congo red staining. It was also positively stained with both anti‐κ and ‐λ light chain antibodies. Moreover, the cytoplasm of the infiltrating plasma cells also positively reacted to both antibodies. The major amyloid proteins of primary localized cutaneous nodular amyloidosis (PLCNA) generally consist of monoclonal immunoglobulin light chains. A review of literature demonstrates 13 cases of PLCNA with SjS, in which immunoglobulin light chains were demonstrated in the amyloid in 5 cases. Amyloid in the 3 cases was composed of a single class immunoglobulin light chain and that in the 2 cases was composed of both κ and λ light chains. Polyclonal immunoglobulin amyloid has been reported only in PLCNA with SjS, which may be related to the fact that a certain population of SjS develops polyclonal B cell proliferation and hyperglobulinemia.     

Nodular localized primary cutaneous amyloidosis

The most common forms of localized primary cutaneous amyloidosis are lichen (papular) and macular amyloidosis. Nodular or tumefactive amyloidosis is rare and demonstrates important clinical, historical, pathogenic and prognostic differences from the lichen and macular variants. We report two cases of nodular localized primary cutaneous amyloidosis.     

Amyloid in localized cutaneous amyloidosis: immunofluorescence studies with anti-keratin antiserum especially concerning the difference between systemic and localized cutaneous amyloidosis

Amyloid of localized cutaneous amyloidosis and systemic amyloidosis were subjected to study with an indirect immunofluorescence technique using anti-keratin antiserum. Anti-keratin antiserum was prepared ad modum Sun & Green. Amyloid of localized cutaneous amyloidosis was positively stained for the antiserum, whereas amyloid of systemic amyloidosis (primary and multiple myeloma-associated) was negative. There was no difference between primary localized cutaneous amyloidosis (lichen amyloidosus and macular amyloidosis) and secondary localized cutaneous amyloidosis (amyloidosis associated with skin tumor). These results indicate that amyloid of localized cutaneous amyloidosis contains components derived from epidermal fibrous protein, probably tonofilaments of keratinocytes.     

Advanced glycation end product-modified beta2-microglobulin is a component of amyloid fibrils of primary localized cutaneous nodular amyloidosis

Primary localized cutaneous nodular amyloidosis is a rare form of cutaneous amyloidosis. Amyloid fibrils in primary localized cutaneous nodular amyloidosis have been reported to be originated from immunoglobulin light chains. Immunohistochemical studies on the lesional skins of four patients with primary localized cutaneous nodular amyloidosis demonstrated that amyloid deposits of all cases showed a positive reaction with the antibodies for beta2-microglobulin and advanced glycation end products as well as immunoglobulin light chain (kappa or lambda). No beta2-microglobulin and advanced glycation end product immunoreactivity was found in the amyloid deposits of other primary localized cutaneous amyloidosis (lichen amyloidosis and macular amyloidosis). Double immunofluorescence study of the lesional skin of primary localized cutaneous nodular amyloidosis showed that anti-kappa light chain, anti-beta2-microglobulin and anti-advanced glycation end product antibodies mostly reacted with the same area of amyloid deposit. Amyloid proteins were sequentially extracted with distilled water from one case of primary localized cutaneous nodular amyloidosis and recovered in the five water-soluble fractions (fractions I-V). Immunoblot assay of amyloid fibril proteins demonstrated that immunoreactive polypeptides with anti-kappa light chain antibody (29 kDa) and with anti-beta2-microglobulin antibody (12 kDa) were detected in fractions I-V, whereas immunoreactive polypeptide with anti-advanced glycation end product antibody (12 kDa) was detected exclusively in fractions III-V but not in fractions I and II. Two-dimensional polyacrylamide gel electrophoresis revealed that 12 kDa polypeptide in fractions I and II was electrophoretically identical with authentic beta2-microglobulin and that beta2-microglobulin in fractions III-V was advanced glycation end product-modified beta2-microglobulin with more acidic pI value. These results indicate that beta2-microglobulin is another major component of amyloid fibrils in primary localized cutaneous nodular amyloidosis and that beta2-microglobulin in primary localized cutaneous nodular amyloidosis is partly subjected to the modification of advanced glycation end product.     

Gene rearrangement studies in the diagnosis of primary systemic and nodular primary localized cutaneous amyloidosis

Difficulties may arise in the diagnosis of patients with clinical features suggestive of plasma cell dyscrasia-related amyloidosis (amyloidosis L), but without evidence of a paraprotein. We have employed gene rearrangement methodology to demonstrate the clonality of bone marrow cells not only in a patient with myeloma-associated systemic amyloidosis, but also in a patient with "primary" systemic amyloidosis without overt myeloma or a detectable paraprotein. Furthermore, we have shown the clonality of the amyloid-producing plasma cells within a skin nodule of a patient with primary localized cutaneous amyloidosis; by contrast, clonal rearrangement was not detected in bone marrow cells from this patient. This finding provides definitive proof that organ-limited nodular primary localized cutaneous amyloid deposits arise in relation to cutaneous plasmacytomas. Gene rearrangement studies may enable early diagnosis and initiation of treatment in patients with systemic amyloidosis L, as well as their differentiation from patients with organ-limited nodular cutaneous amyloidosis, who do not require aggressive therapy.     

Primary Localized Cutaneous Nodular Amyloidosis Following Local Trauma

Primary localized cutaneous nodular amyloidosis (nodular amyloidosis) is a rare and distinct type of amyloidosis, in which amyloid L deposition is limited to the skin and typically manifested as a tumefactive nodule on the acral sites. However, the definite cause of nodular amyloidosis is still unknown. Although it is relatively well known that the amyloid deposits in nodular amyloidosis originate from immunoglobulin light chains secreted by local plasma cells, traumatic injury to the skin has rarely been recognized as a triggering factor of nodular amyloidosis. Herein, we present a case of a 50-year-old male patient with primary localized cutaneous nodular amyloidosis, which occurred after local trauma, and discuss the relationship between traumatic damage and dermal amyloid L deposition.     

Primary Localized Cutaneous Amyloidosis in Association with Papillary Thyroid Carcinoma

Background: Lichen amyloidosis, a type of primary localized cutaneous amyloidosis, is characterized by pruritic brown or grayish pigmented papules. Objective: We report a case of lichen amyloidosis in which the skin lesion consisted of asymptomatic salmon-pink-colored papules on the back of the neck to the upper back. This was different from typical clinical pictures of lichen amyloidosis. Our patient proved to have thyroid papillary carcinoma. Conclusion: Our case may suggest that lichen amyloidosis could be a cutaneous manifestation of thyroid cancers.     

Lichen amyloidosis,ankylosing spondylitis and autoimmune thyroiditis: coincidence or association?

Primary localized cutaneous amyloidosis (PLCA) is characterized by the deposition of amyloid in a previously apparently normal skin with the absence of other systemic or cutaneous disorder. Although ankylosing spondylitis may be associated with secondary systemic amyloidosis, no reports have been found showing the association of this disease with PLCA. In addition, the association of PLCA with autoimmune thyroiditis has not been previously reported. We report a concomitant occurrence of lichen amyloidosis, ankylosing spondylitis and autoimmune thyroiditis in a caucasian woman.     

Nodular primary localized cutaneous amyloidosis: immunohistochemical evaluation and treatment with the carbon dioxide laser

Nodular primary localized cutaneous amyloidosis is an uncommon disorder for which there is no consistently satisfactory treatment. The amyloid fibrils are thought to have an immunoglobulin light chain derivation and systemic involvement must be excluded in all cases. We report a patient with a large scalp lesion of nodular primary localized cutaneous amyloidosis whose immunohistochemical evaluation revealed lambda light chain deposits and who thus far has no apparent systemic involvement. The lesion was treated by the carbon dioxide (CO2) laser with excellent cosmetic results and minimal morbidity.     

Nodular amyloidosis: Case report and literature review

BACKGROUND: Amyloidosis refers to a group of depositional diseases that are classified into two main types: systemic and localized. Large nodules of localized cutaneous amyloidosis of the nasal ala and surrounding skin are rare and the treatment is often unsatisfactory. OBJECTIVE: We report a case of rapidly enlarging, localized, nodular cutaneous amyloidosis of the nose and the surrounding skin with a brief review of the current literature regarding treatment of this rare disease. CONCLUSION: Nodular amyloidosis can be treated successfully with cold steel excision in combination with carbon dioxide laser. Close followup of these patients is warranted, as nodular amyloidosis may be the precursor to systemic amyloidosis.     

Nodular cutaneous amyloidosis involving the vulva. Case report and literature review

A case of localized nodular cutaneous amyloidosis involving the vulva occurred in a 53-year-old woman. This rare type of cutaneous amyloidosis has been reported in the female genitalia in two prior cases. The unusual aspects of our case were (1) recurrence after six years, (2) an ulcerative appearance clinically simulating a malignant neoplasm, and (3) the presence of numerous Russell bodies. Our histopathologic findings in hematoxylin-eosin-and peroxidase-antiperoxidase-stained sections support the concept of immunoglobulin light chain derivation.     

Amiloidosis cutánea primaria localizada nodular con patrón diseminado

Amyloid is a proteinaceous material that is deposited in the tissues in a large variety of clinical contexts; in the skin it can be found with or without concomitant systemic disease. Primary localized cutaneous amyloidosis encompasses those amyloidoses restricted to the skin without involvement of other systems. The most common forms within this group are macular and lichen amyloidosis. Nodular amyloidosis is extremely rare, and there are notable differences in clinical presentation, prognosis, histology, and pathogenesis between this entity and the macular and lichenoid variants.We report a new case of nodular primary localized cutaneous amyloidosis with disseminated plaques and nodules in which no systemic disease developed in the 3 years following the appearance of the lesions.     

Case of primary localized cutaneous amyloidosis with protean clinical manifestations: lichen, poikiloderma-like, dyschromic and bullous variants

Primary localized cutaneous amyloidosis (PLCA) commonly presents as macular and lichen variants. We present a case of a 27-year-old Chinese woman with cutaneous features of the rarely reported poikiloderma-like, dyschromic and bullous forms of PLCA, and the commoner lichen variant. There were no syndromic associations or systemic involvement, and the various morphological subtypes occurred in isolation from one another. We review the clinical spectrum of PLCA, highlight its protean clinical manifestations in this patient, and discuss its postulated pathogenesis in relation to its histopathological features.     

Nodular localized primary cutaneous amyloidosis: a bullous variant

Primary cutaneous amyloidosis describes a group of disorders in which amyloid is deposited in the skin without evidence of systemic involvement. Nodular localized primary cutaneous amyloidosis (NLPCA) is a rare form of these skin‐restricted amyloidoses. We present an unusual case of NLPCA in a 51‐year‐old man, who had clinical and histopathological evidence of subepidermal bullous formation, a unique feature in NLPCA. The possible pathogenesis of this change is discussed.     

Primary cutaneous amyloidosis of the external ear: a clinicopathological and immunohistochemical study of 17 cases

Primary cutaneous amyloidosis includes several forms of localized amyloidosis characterized by superficial amyloid deposits occurring at or near the dermal–epidermal junction in the absence of systemic involvement. Primary cutaneous amyloidosis of the auricular concha and external ear represents a rarely described variant. There have been 27 cases reported in the English language literature, and herein we report 17 additional cases. This article demonstrates that the amyloid observed in this context is generally positive for Congo red, crystal violet and thioflavin T. It also expresses cytokeratin 34ßE12 via immunohistochemistry. Our immunohistochemical results and review of the literature suggest that the amyloid in amyloidosis of the external ear is the result of basal keratinocyte degeneration and does not signify deposition from a systemic or generalized process. Wenson SF, Jessup CJ, Johnson MM, Cohen LM, Mahmoodi M. Primary cutaneous amyloidosis of the external ear: a clinicopathological and immunohistochemical study of 17 cases.     

Localized amyloidosis of the glans penis: a case report and literature review

BACKGROUND: Primary localized cutaneous amyloidosis is an uncommon lesion with a varied pathogenesis. METHODS: We report the case of a 67-year-old-male discovered to have a localized amyloid lesion of the glans penis. RESULTS: Biopsy of the lesion revealed dermal deposits of amorphous eosinophilic material which stained positive with Congo red and amyloid P protein. Additional stains, including kappa and lambda light chains, amyloid A, and transthyretin, were negative. The lesion has remained asymptomatic, with no evidence of systemic disease identified, and no further treatment has been necessary. CONCLUSIONS: This is the sixth reported case of localized amyloidosis of the glans penis. Based on the clinical behavior and pathologic characteristics, this type of lesion is best classified as primary localized cutaneous amyloidosis, in the same family as the macular/lichenoid type lesions.     

Localized primary cutaneous nodular amyloidosis: case report

Amyloidosis results from deposition of fibrous and insoluble amyloid protein in extracellular spaces of organs and tissues. Amyloid deposition can be localized or systemic and either primary or secondary. We report a case of localized primary cutaneous nodular amyloidosis manifested by papular-nodular, reddish-brown lesions affecting the nasal area, without evidence of systemic involvement. Immunohistochemistry showed the presence of immunoglobulin kappa light chain.     

Nylon cloth macular amyloidosis

In primary localized cutaneous amyloid, deposition of amyloid is confined to the skin without the involvement of any internal organs. Amyloid deposition in the skin is often scanty, and electron microscopy may be needed to confirm the presence of the typical amyloid fibrils. There have been several case reports of cutaneous amyloidosis associated with friction or rubbing of the skin. We report a case of primary localized cutaneous amyloid associated with the habitual use of a nylon cloth.     

Unusual primary cutaneous localized amyloidosis

The case of a 41-year-old female patient with an unusual type of primary localized cutaneous amyloidosis is reported. Clinical examination revealed lesions typical for macular cutaneous amyloidosis, while histology and histochemistry, in contrast, revealed the presence of nodular amyloidosis of the skin with deposition of lambda light chain amyloid.