Monoclonal antibody to a common antigen of secretory granule membranes: intracellular localization and recycling of the antigen after secretion.

Yamashita, Shuji; Yasuda, Kazuto

doi:10.1177/40.6.1588026

Cited by 5 publications

(1 citation statement)

References 6 publications

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“…The results presented here indicate that the autoantigen of IDDM ICA 512 is an intrinsic membrane protein of peptide-containing secretory granules of endocrine cells and neurons. ICA 512 joins a growing list of transmembrane proteins of secretory granules, including vacuolar type proton-pumping ATPase (Nelson and Lill, 1994), cytochrome b561 (Silsand and Flatmark, 1974), nucleotide carrier (Kostron et al, 1977), vesicular amine transporter (VAT) (Erickson et al, 1992), SV2 (Lowe et al, 1988;Feany et al, 1992) peptidyl a-amidating monooxygenase (PAM) (Eipper et al, 1993), glycoprotein II (Obendorf et al, 1988), synaptophysin (Lowe et al, 1988), synaptotagmin (Lowe et al, 1988;Walch-Solimena et al, 1993), synaptobrevins (Chilcote et al, 1995), secretory carrier membrane proteins (SCAMPs) (Brand et al, 1991, Brand andCastle, 1993) and secretory granule-specific antigen (SGSA) (Yamashita and Yasuda, 1992). Several features, however, distinguish ICA 512 from other constituents of secretory granule membranes.…”

Section: Discussionmentioning

confidence: 99%

ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules.

et al. 1996

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Islet cell autoantigen (ICA) 512 is a novel autoantigen of insulin‐dependent diabetes mellitus (IDDM) which is homologous to receptor‐type protein tyrosine phosphatases (++PTPases). We show that ICA 512 is an intrinsic membrane protein of secretory granules expressed in insulin‐producing pancreatic beta‐cells as well as in virtually all other peptide‐secreting endocrine cells and neurons containing neurosecretory granules. ICA 512 is cleaved at its luminal domain and, following exposure at the cell surface, recycles to the Golgi complex region and is sorted into newly formed secretory granules. By immunoprecipitation, anti‐ICA 512 autoantibodies were detected in 15/17 (88%) newly diagnosed IDDM patients, but not in 10/10 healthy subjects. These results suggest that tyrosine phosphorylation participates in some aspect of secretory granule function common to all neuroendocrine cells and that a subset of autoantibodies in IDDM is directed against an integral membrane protein of insulin‐containing granules.

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Section: Discussionmentioning

confidence: 99%

ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules.

et al. 1996

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Recycling of a secretory granule membrane protein after stimulated secretion

Hurtley

1993

Journal of Cell Science

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Recycling of a secretory granule membrane protein, dopamine-beta-hydroxylase, was examined in primary cultures of bovine adrenal chromaffin cells. Cells were stimulated to secrete in the presence of antibodies directed against the luminal domain of dopamine-beta-hydroxylase. The location of the antibodies after various times of reincubation and after a second secretory stimulus was assessed using immunofluorescence microscopy. Stimulation led to the exposure of dopamine-beta-hydroxylase at the plasma membrane, which could be detected by a polyclonal antibody in living and fixed cells. The plasma membrane dopamine-beta-hydroxylase, either alone or complexed with antibody, was rapidly internalized after removal of the secretagogue. Internalized protein-antibody complex remained stable for at least 24 hours of reculture. Twenty four hours after stimulation the cells with internalized antibody could respond to further stimulation and some of the antibody was re-exposed at the plasma membrane. These findings were confirmed using FACS analysis. This suggests that the antibody-protein complex had returned to secretory granules that could respond to further secretagogue stimulation.

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Two proteins associated with secretory granule membranes identified in chicken regulated secretory cells

Thomas

Stieber

Gonatas

1994

Journal of Cell Science

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Lately, we have identified two polypeptides of 92–94 kDa (GRL1) and 45–60 kDa (GRL2), expressed in cytoplasmic granules of chicken granulocytes and thrombocytes. Here, we report that GRL1 and GRL2 are widely distributed in all exocrine and several endocrine cell types, but not in neurons of the central nervous system, during late stages of embryonic development, as well as in newly hatched and two-month-old chickens. Immunogold studies in ultrathin frozen sections of pancreatic acinar cells show that GRL1 and GRL2 are co-localized at the periphery of zymogen granules, in granules fused with apical acinar membranes and on apical membranes of acini, while the pregranular compartments of the secretory pathway are weakly or not labeled. Semiquantitative morphometric studies indicate that GRL1 and GRL2 are equally distributed in secretory granules. A variety of physical and metabolic studies reveal that GRL2, a highly N-glycosylated polypeptide, is an intrinsic membrane protein, while GRL1 is a peripheral membrane polypeptide released by Na2CO3 treatment of granulocyte membranes. In all hematopoietic, exocrine or endocrine cells examinated, GRL1 shows identical electrophoretic patterns, while GRL2 is identified as a diffuse band, at 40–65 kDa, in hematopoietic and pancreatic cells. Taken together, the morphological and biochemical studies indicate that GRL1 and GRL2 are components of the secretory granule membrane in chicken exocrine, endocrine and hemopoietic cell types.

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Monoclonal antibody to a common antigen of secretory granule membranes: intracellular localization and recycling of the antigen after secretion.

Cited by 5 publications

References 6 publications

ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules.

ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules.

Recycling of a secretory granule membrane protein after stimulated secretion

Two proteins associated with secretory granule membranes identified in chicken regulated secretory cells

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