The role of immunoglobulin heavy chain binding protein: in immunoglobulin transport |
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| Affiliation: | 1. Discipline of Medical Biochemistry, College of Medicine and Public Health, Flinders University, Adelaide, South Australia, Australia;2. Discipline of Human Physiology, College of Medicine and Public Health, Flinders University, Adelaide, South Australia, Australia;3. The HPB and Liver Transplant Unit, Flinders Medical Centre and College of Medicine and Public Health, Flinders University, Adelaide, South Australia, Australia;4. Department of Surgery, Isala, Zwolle, The Netherlands;1. Institute of Experimental Physiology (IFISE-CONICET), Suipacha 570, 2000 Rosario, Argentina;2. University of Connecticut, School of Pharmacy, Department of Pharmaceutical Sciences, Storrs, CT, USA;3. Institute of Pharmacological Investigations (ININFA-CONICET), University of Buenos Aires, Buenos Aires, Argentina;4. Department of Clinical Pharmacology and Pharmacoepidemiology, University of Heidelberg, Heidelberg, Germany |
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| Abstract: | ![]()
More than ten years ago a heavy chain binding protein (BiP) was described which is associated with immunoglobulin heavy chains (HC) within the endoplasmic reticulum (ER) [which is the site of Immunoglobulin (Ig) assembly].Recently, Linda Hendershot and her collegues suggested that BiP might combine with nascent HC as they enter the ER and hold them there until assembly with light chain (LC) occurs. In the absence of LC synthesis or assembly, the HC would remain associated with BiP and would eventually be degraded internally.They now propose a means for BiP to block the transport of unassembled Ig molecules. Transport of protein from ER to the Golgi apparatus seems to be mediated by transport signals inherent to the protein molecule itself. Ig transport signals have been thought to be on the LC because LC can be secreted alone while HC cannot under normal circumstances. When BiP is displaced by LC, completed Ig molecules are transported.They use this model to explain regulated transport of Ig molecules during B-cell development, and suggest that BiP may be post-translationally associated with the nascent chains of other membrane and secretory proteins before folding or subunit assembly. |
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