Cytoplasmic Carbonic Anhydrase II of Rat Coagulating Gland Is Secreted via the Apocrine Export Mode

Wilhelm, Beate; Keppler, Claudia; Hoffbauer, Gudrun; Lottspeich, Friedrich; Linder, Dietmar; Meinhardt, Andreas; Aumüller, Gerhard; Seitz, Jürgen

doi:10.1177/002215549804600410

Cited by 32 publications

(30 citation statements)

References 29 publications

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“…Because the guinea pig cDNAs for Prkg2 and CFTR had not been cloned yet, the examinations were focused on guanylin, uroguanylin, Gucy2c, and Slc4a2. At the translational level, the presence of all these proteins in the liver and gallbladder were confirmed by immunoblotting experiments with a panel of protein-domain-specific antisera demonstrating proteins of correct molecular weights as deduced from the respective cDNA (Kulaksiz et al 2001b(Kulaksiz et al , 2002aWilhelm et al 1998). As already described in former publications, an additional immunoreactive band arose for guanylin with a molecular mass between 17 and 19 kDa.…”

Section: Discussionsupporting

confidence: 65%

“…1g). The region-specific Car2-antiserum (Wilhelm et al 1998) detected the protein at *29 kDa molecular mass in the extracts of lung (rat, positive control), liver and gallbladder (Fig. 1h).…”

Section: Resultsmentioning

confidence: 95%

“…The antisera generated and used were here K42 directed against proguanylin (aa 34-46), K605 directed against proguanylin (aa 101-115), K735 recognizing Gucy2c (aa 31-45) and K741 recognizing Gucy2c (aa 1,009-1,023), EG(1)-PKIIA directed against PRKG2 (aa 146-158), EG(2)-CFTR122 recognizing CFTR (aa 122-136), EG(1)-AE2 recognizing SLC4A2 (aa 1,217-1,239), and anti-CAHII (Kulaksiz et al 2001b;Wilhelm et al 1998) directed against Car2.…”

Section: Peptides and Antibodiesmentioning

confidence: 99%

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Guanylin and functional coupling proteins in the hepatobiliary system of rat and guinea pig

Schwabe

Cetin

2012

Histochem Cell Biol

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Guanylin, a bioactive intestinal peptide, is involved in the cystic fibrosis transmembrane conductance (CFTR)-regulated electrolyte/water secretion in various epithelia. In the present work we report on the expression and cellular localization of guanylin and its affiliated signaling and effector proteins, including guanylate cyclase C (Gucy2c), Proteinkinase GII (Pkrg2), CFTR and the solute carrier family 4, anion exchanger, member 2 (Slc4a2) in the hepatobiliary system of rat and guinea pig. Localization studies in the liver and the gallbladder revealed that guanylin is located in the secretory epithelial cells of bile ducts of the liver and of the gallbladder, while Gucy2c, Pkrg2, CFTR, and Slc4a2 are confined exclusively to the apical membrane of the same epithelial cells. Based on these findings, we assume that guanylin is synthesized as an intrinsic peptide in epithelial cells of the hepatobiliary system and released luminally into the hepatic and cystic bile to regulate electrolyte secretion by a paracrine/luminocrine signaling pathway.

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Section: Discussionsupporting

confidence: 65%

Section: Resultsmentioning

confidence: 95%

Section: Peptides and Antibodiesmentioning

confidence: 99%

See 1 more Smart Citation

Guanylin and functional coupling proteins in the hepatobiliary system of rat and guinea pig

Schwabe

Cetin

2012

Histochem Cell Biol

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“…In 1988, Agrawal and Vanha-Perttula described a release of membrane-bound vesicles into the secretory fl uid of the lumen of the bovine epididymis [Agrawal and Vanha-Perttula, 1988]. The concept for a non-classical route of protein secretion, also known as 'apocrine secretion', has already been proposed for different parts of the male reproductive tract, e.g., the coagulating gland and the dorsal prostate of the rat [Seitz et al, 1990;Aumüller et al, 1991;Steinhoff et al, 1994;Wilhelm et al, 1998], as well as the seminal vesicle and the ductus deferens [Kaunisto et al, 1990;Manin et al, 1995]. The MIF-containing luminal vesicles were localized in close contact to the luminal sperm cells ( fi g. 4 C).…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical Detection of Macrophage Migration Inhibitory Factor in Fetal and Adult Bovine Epididymis: Release by the Apocrine Secretion Mode?

Eickhoff

Jennemann

Hoffbauer

et al. 2006

Cells Tissues Organs

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Originally defined as a lymphokine inhibiting the random migration of macrophages, the macrophage migration inhibitory factor (MIF) is an important mediator of the host response to infection. Beyond its function as a classical cytokine, MIF is currently portrayed as a multifunctional protein with growth-regulating properties present in organ systems beyond immune cells. In previous studies, we detected substantial amounts of MIF in the rat epididymis and epididymal spermatozoa, where it appears to play a role during post-testicular sperm maturation and the acquisition of fertilization ability. To explore its presence in other species not yet examined in this respect, we extended the range of studies to the bull. Using a polyclonal antibody raised against MIF purified from bovine eye lenses, we detected MIF in the epithelium of the adult bovine epididymis with the basal cells representing a prominently stained cell type. A distinct accumulation of MIF at the apical cell pole of the epithelial cells and in membranous vesicles localized in the lumen of the epididymal duct was obvious. In the fetal bovine epididymis, we also detected MIF in the epithelium, whereas MIF accumulation was evident at the apical cell surface and in apical protrusions. By immunoelectron microscopy of the adult bovine epididymis, we localized MIF in apical protrusions of the epithelial cells and in luminal membrane-bound vesicles that were found in close proximity to sperm cells. Although the precise origin of the MIF-containing vesicles remains to be delineated, our morphological observations support the hypothesis that they become detached from the apical surface of the epididymal epithelial cells. Additionally, an association of MIF with the outer dense fibers of luminal spermatozoa was demonstrated. Data obtained in this study suggest MIF release by an apocrine secretion mode in the bovine epididymis. Furthermore, MIF localized in the basal cells of the epithelium and in the connective tissue could be responsible for regulating the migration of macrophages in order to avoid contact of immune cells with spermatozoa that carry a wide range of potent antigens.

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“…Monoclonal mouse antibodies against human cytokeratin 18 (DC-10) and 19 (A53-B/A2) were from Santa Cruz Biotechnology (Santa Cruz, Calif., USA). Rabbit polyclonal antibodies against human and rat carbonic anhydrase II (CAII) were a gift of J. Seitz (Philipps University, Marburg), which have already been used and characterized (Wilhelm et al 1998).…”

mentioning

confidence: 99%

Guanylin in the human pancreas: a novel luminocrine regulatory pathway of electrolyte secretion via cGMP and CFTR in the ductal system

Kulaksiz

Schmid

Hönscheid

et al. 2001

Histochem Cell Biol

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Cystic fibrosis transmembrane conductance regulator (CFTR) is a channel and regulator protein that is crucially involved in transepithelial ion transport. In the exocrine pancreas, the CFTR-mediated secretion of an electrolyte-rich fluid is a major but as yet incompletely understood function. We show here that the peptide guanylin is a specific activator of CFTR function in the human pancreas implicating regulation of pancreatic electrolyte secretion. Guanylin and its affiliated signaling and effector proteins including guanylate cyclase C, cGMP-dependent protein kinase II, CFTR, and the epithelial Cl-/HCO3- exchanger, anion exchanger 2, are highly expressed in the human pancreas. Guanylin is localized specifically to the typical centroacinar cells and proximal duct cells which, based on its additional presence in the pancreatic juice, is obviously released luminally into the pancreatic ducts. The guanylin receptor and the respective functional downstream proteins are all confined to the apical membrane of the duct cells implicating an as yet unknown route of luminal regulatory pathway of electrolyte secretion in the ductal system. Functional studies in two different human pancreatic duct cell lines expressing the CFTR Cl- channel that is functionally intact in CAPAN-1 cells but defective (delta F508) in CFPAC-1 cells clearly identify guanylin as a specific regulator of pancreatic CFTR channel function. Whole-cell patch-clamp recordings in CAPAN-1 cells revealed that forskolin induces an increase of Cl- conductance mediated by cAMP. In contrast, guanylin increased Cl- conductance in the same cells via cGMP but not cAMP; the respective membrane current was largely blockable by the sulfonylurea glibenclamide. In CFPAC-1 cells, however, neither guanylin nor forskolin produced a current activation. Based on the present findings we conclude that guanylin is an intrinsic pancreatic regulator of Cl- current activation in pancreatic duct cells via cGMP and CFTR. Remarkably, in the pancreas guanylin may exert its function through an intriguing luminocrine mode via the pancreatic juice.

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Cytoplasmic Carbonic Anhydrase II of Rat Coagulating Gland Is Secreted via the Apocrine Export Mode

Cited by 32 publications

References 29 publications

Guanylin and functional coupling proteins in the hepatobiliary system of rat and guinea pig

Guanylin and functional coupling proteins in the hepatobiliary system of rat and guinea pig

Immunohistochemical Detection of Macrophage Migration Inhibitory Factor in Fetal and Adult Bovine Epididymis: Release by the Apocrine Secretion Mode?

Guanylin in the human pancreas: a novel luminocrine regulatory pathway of electrolyte secretion via cGMP and CFTR in the ductal system

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