Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells

نویسندگان

  • K Buckley
  • R B Kelly
چکیده

Several types of cells store proteins in secretory vesicles from which they are released by an appropriate stimulus. It might be expected that the secretory vesicles in different cell types use similar molecular machinery. Here we describe a transmembrane glycoprotein (Mr approximately 100,000) that is present in secretory vesicles in all neurons and endocrine cells studied, in species from elasmobranch fish to mammals, and in neural and endocrine cell lines. It was detected by cross-reactivity with monoclonal antibodies raised to highly purified cholinergic synaptic vesicles from the electric organ of fish. By immunoprecipitation of intact synaptic vesicles and electron microscopic immunoperoxidase labeling, we have shown that the antigenic determinant is on the cytoplasmic face of the synaptic vesicles. However, the electrophoretic mobility of the antigen synthesized in the presence of tunicamycin is reduced to Mr approximately 62,000, which suggests that the antigen is glycosylated and must therefore span the vesicle membrane.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Secretory Vesicle and Cell Surface Markers for Human Endocrine Pancreatic and Pituitary Tumors

9 1992 Blackwell Scientific Publications, Inc. The pancreatic islet and the adenohypophysis are endocrine tissues sharing several properties. These organs are both composed of different endocrine cells secreting a variety of hormones. These are stored within the cells in dense core secretory vesicles and are released by appropriate stimuli. In addition to dense core secretory vesicles, endocrin...

متن کامل

Protein Profiling of the Secretome of FcεRI Activated RBL-2H3.1 Cells

Background: Secretory proteins of IgE receptor activated mast cells and basophils play a pivotal role in the generation of immediate and long term immune responses in allergy and type I hypersensitivity. Objective: The present study aims to generate a 2-D map and profile of proteins secreted from a high secretory variant of the rat basophilic leukemia cell line, RBL-2H3.1, which in view of the ...

متن کامل

Identification of a Chromogranin A Domain That Mediates Binding to Secretogranin III and Targeting to Secretory Granules in Pituitary Cells and Pancreatic -Cells

Chromogranin A (CgA) is transported restrictedly to secretory granules in neuroendocrine cells. In addition to pHand Ca2 -dependent aggregation, CgA is known to bind to a number of vesicle matrix proteins. Because the binding-prone property of CgA with secretory proteins may be essential for its targeting to secretory granules, we screened its binding partner proteins using a yeast two-hybrid s...

متن کامل

Cytochemical identification of endocrine thymus of chicken in relation to aging

Age related cytochemical changes of thymic endocrine cells were studied in 78 day old chicks at five day interval to age of day 60 employing a panel of cytochemical stains. Methenamine silver revealed cell morphology including cell processes distinctly while diamine silver revealed a stronger argentaffinity in these cells. The cells had greater affinity for diamine silver compared to methenamin...

متن کامل

The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: studies by gene transfer

The exocrine protein rat anionic trypsinogen has been expressed and is secreted from the murine anterior pituitary tumor cell line AtT-20. We examined which secretory pathway trypsinogen takes to the surface of this endocrine-derived cell line. The "constitutive" pathway externalizes proteins rapidly and in the absence of an external stimulus. In the alternate, "regulated" pathway, proteins are...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Journal of Cell Biology

دوره 100  شماره 

صفحات  -

تاریخ انتشار 1985