Immunological characterization of chromogranins A and B and secretogranin II in the bovine pancreatic islet

Souma, Yoshie; Hagn, C.; Ehrhart, M.; Fischer‐Colbrie, Reiner; Grube, D.; Winkler, Hans; Gratzl, Manfred

doi:10.1007/bf00533393

Cited by 40 publications

(11 citation statements)

References 40 publications

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“…Many authors conclude that the best diluent buffer for MAbs and PAbs is 0.05 to 0.1 M Tris buffer (pH 6.0), but there are exceptions. 31,33,429 Tris buffer should also be used for alkaline phosphatase procedures, because the high concentration of inorganic phosphate competes for the phosphatase. 89 Background reactivity due to ionic interactions can be reduced by increasing the NaCl concentration in the buffer to 0.3 to 0.5 M; 277 however, increased ionic strength can disrupt the binding of specific but low-affinity antibodies, so it should be used judiciously.…”

Section: Diluent Buffermentioning

confidence: 99%

When Tissue Antigens and Antibodies Get Along

2013

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Once focused mainly on the characterization of neoplasms, immunohistochemistry (IHC) today is used in the investigation of a broad range of disease processes with applications in diagnosis, prognostication, therapeutic decisions to tailor treatment to an individual patient, and investigations into the pathogenesis of disease. This review addresses the technical aspects of immunohistochemistry (and, to a lesser extent, immunocytochemistry) with attention to the antigen-antibody reaction, optimal fixation techniques, tissue processing considerations, antigen retrieval methods, detection systems, selection and use of an autostainer, standardization and validation of IHC tests, preparation of proper tissue and reagent controls, tissue microarrays and other high-throughput systems, quality assurance/quality control measures, interpretation of the IHC reaction, and reporting of results. It is now more important than ever, with these sophisticated applications, to standardize the entire IHC process from tissue collection through interpretation and reporting to minimize variability among laboratories and to facilitate quantification and interlaboratory comparison of IHC results.

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Section: Diluent Buffermentioning

confidence: 99%

When Tissue Antigens and Antibodies Get Along

2013

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“…Cohn et al, 1984;Wilson and Lloyd, 1984;O'Connor, 1983). lmmunohistochemical studies of bovine endocrine pancreas have demonstrated that chromogranin A is present in cells producing insulin (B-cells), glucagon (A-cells), and somatostatin (D-cells) and in a few cells containing pancreatic polypeptide (PP-cells) (Yoshie et al, 1987;Ehrhart et al, 1986). Chromogranin A is co-stored in the same secretory granules as the established hormones (Ehrhart et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Cellular distribution and amount of chromogranin A in bovine endocrine pancreas.

Ehrhart¹,

Jörns²,

Grube³

et al. 1988

J Histochem Cytochem.

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We determined the cellular distribution and the amount of chromogranin A in endocrine cells of bovine pancreas using a polyclonal antibody against bovine adrenomedullary chromogranin A. The relative amounts of chromogranin A in the different cells of the endocrine pancreas were determined by computer-assisted analyses of the optical densities of the immunoreactivities in the stained sections. More than 80% of the immunoreactive chromogranin A was located in the pancreatic B-cells. In immunoblots of acid tissue extracts, only one chromogranin A band (MW 74 KD) was observed. Quantification of the immunoblots revealed that 3 micrograms of chromogranin A and 918 micrograms of insulin were present per gram pancreas (wet weight), equivalent to a molar ratio of 460 mumol chromogranin A per mol insulin.

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“…The presence of a n identical protein was subsequently demonstrated in adrenal medullary chromaffin cells (2). In fact like other members of the chromogranin family, SgII has a widespread distribution, being present in the matrix of secretory granules of a variety of endocrine and neuronal cells including pituitary (I), pancreatic islets (25) and endocrine cells of the gut (26). In neuronal tissue, SgII has been identified in the hippocampus (3), the cerebellum (6) and the splenic nerve (27).…”

Section: Discussionmentioning

confidence: 99%

Secretogranin II: Regulation of Synthesis and Post‐Translational Proteolysis in Bovine Adrenal Chromaffin Cells

Soszynski

Metz‐Boutigue

Aunis

et al. 1993

J Neuroendocrinology

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Secretogranin II (SgII), also called chromogranin C, is an acidic tyrosine-sulfated secretory protein found in secretory granules in a wide variety of endocrine cells and neurones. Although less abundant than chromogranin A (CGA) and chromogranin B (CGB), SgII is found in adrenal medullary chromaffin granules. In the present study we investigated the regulation of SgII biosynthesis in bovine chromaffin cells maintained in primary culture. Cellular proteins were labelled with [35S]methionine and the heat stable chromogranin enriched fraction was isolated. Following electrophoretic separation, the 86 kDa SgII band was identified by sequence analysis using the Edman degradation procedure. The radioactivity incorporated in the 86 kDa SgII band was used as an index of the SgII synthesis rate. We found that stimulation of chromaffin cells with nicotine and histamine and to a smaller extent with angiotensin II and bradykinin significantly enhanced the rate of SgII synthesis. In contrast direct depolarization with K+ may not be sufficient to induce modifications in SgII synthesis suggesting that the raise of cytosolic calcium evoked by high K+ may not be sufficient to induce modifications in SgII synthesis . The possible second messenger pathways involved in the control of SgII biosynthesis were investigated by using protein kinase C and adenylate cyclase activators. We observed that 12-O-tetradecanoylphorbol 13-acetate (TPA) and forskolin increased the basal rate of SgII synthesis. Incubation with both TPA and forskolin was required to obtain an effect comparable to that produced by nicotine or histamine suggesting that these secretagogues recruit both protein kinase C- and cyclic AMP-dependent mechanisms to stimulate SgII synthesis.

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Immunological characterization of chromogranins A and B and secretogranin II in the bovine pancreatic islet

Cited by 40 publications

References 40 publications

When Tissue Antigens and Antibodies Get Along

When Tissue Antigens and Antibodies Get Along

Cellular distribution and amount of chromogranin A in bovine endocrine pancreas.

Secretogranin II: Regulation of Synthesis and Post‐Translational Proteolysis in Bovine Adrenal Chromaffin Cells

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