A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial expression and predicts a novel protein

Kasik, W. John

doi:10.1042/bj3300947

Cited by 17 publications

(15 citation statements)

References 36 publications

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“…In Vivo Expression of Itmap1-Itmap1 was first identified as a novel ZP protein induced specifically in late gestation mouse uterus (6). In accord with this previous report, we found no expression of Itmap1 in non-gravid mouse uterus and high level expression in mid-to-late gestation uterus (Fig.…”

Section: Resultssupporting

confidence: 81%

“…To further understand the mechanisms involved in protecting the acinar cell from digestive damage, we have evaluated the function of a novel acinar cell zona pellucida (ZP) 1 domaincontaining protein Itmap1 (6). ZP domain proteins such as uromodullin, the pancreatic ductal protein muclin, the zymogen granule protein GP2, and the inner ear protein ␤-tectorin are often found in fibrillar or gelatinous compartments of the extracellular matrix, with the ZP domain serving as a filamentorganizing motif (7).…”

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confidence: 99%

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Protection from Pancreatitis by the Zymogen Granule Membrane Protein Integral Membrane-associated Protein-1

Imamura¹,

Asada²,

Vogt

et al. 2002

Journal of Biological Chemistry

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Pancreatitis is a common disease with substantial morbidity and mortality. To better understand the mechanisms conferring sensitivity or resistance to pancreatitis, we have initiated the analysis of novel acinar cell proteins. Integral membrane-associated protein-1 (Itmap1) is a CUB (complement subcomponents C1r/C1s, sea urchin Uegf protein, bone morphogenetic protein-1) and zona pellucida (ZP) domain-containing protein we find prominently expressed in pancreatic acinar cells. Within the acinar cell, Itmap1 localizes to zymogen granule membranes. Although roles in epithelial polarity, granule assembly, and mucosal protection have been postulated for CUB/ZP proteins, in vivo functions for these molecules have not been proven. To determine the function of Itmap1, we generated Itmap1-deficient mice. Itmap1؊/؊ mice demonstrate increased severity of secretagogue-and diet-induced pancreatitis in comparison to Itmap1 ؉/؉ mice. In contrast to previous animal models exhibiting altered severity of pancreatitis, Itmap1 deficiency results in impaired activation of trypsin, an enzyme believed critical for initiating a cascade of digestive zymogen activation during pancreatitis. Itmap1 deficiency does not alter zymogen granule size, appearance, or the composition of zymogen granule contents. Our results demonstrate that Itmap1 plays an essential role in trypsinogen activation and that both impaired and augmented trypsinogen activation can be associated with increased severity of pancreatitis.

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Section: Resultssupporting

confidence: 81%

mentioning

confidence: 99%

Protection from Pancreatitis by the Zymogen Granule Membrane Protein Integral Membrane-associated Protein-1

Imamura¹,

Asada²,

Vogt

et al. 2002

Journal of Biological Chemistry

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“…The other related knockout is of Itmap1 (also known as Cuzd1), which codes a CUB and ZP domaincontaining protein expressed in the exocrine pancreas. Although encoded by a distinct gene, Itmap1 resembles a truncated version of Muclin: it is comprised of two CUB domains, a single ZP domain, a transmembrane domain, and a short COOH-terminal cytosolic tail (27). Itmap1 knockout mice do not have a spontaneous phenotype, but they do exhibit greater severity of experimentally induced pancreatitis, especially when the severe choline-deficient, ethionine-supplemented diet model was used (24).…”

Section: Discussionmentioning

confidence: 99%

Effects of Muclin (Dmbt1) deficiency on the gastrointestinal system

Lisle

Xu²,

Roe³

et al. 2008

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…The localization of the spermligand active high-mannose-type chain in bovine ZPB and ZPC should be clarified. Besides the zona proteins, the ZP domain has been found in several proteins: TGF-b type III receptor (betaglycan) from fetal and adult tissues [28,29], uromodulin (urinary Tamm-Horsfall glycoprotein of pregnant woman) [30], the major zymogen granule membrane protein (GP-2) [31], and the proteins in the uterus and oviduct [32,33]. Furthermore, tectorins in the tectorial membranes responsible for hearing also have a ZP domain [34,35].…”

Section: Discussionmentioning

confidence: 99%

Localization of N‐linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida

Ikeda

Yonezawa

Naoi

et al. 2002

European Journal of Biochemistry

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The zona pellucida, a transparent envelope surrounding the mammalian oocyte, consists of three glycoproteins, ZPA, ZPB and ZPC, and plays a role in sperm-egg interactions. In bovines, these glycoproteins cannot be separated unless the acidic N-acetyllactosamine regions of the carbohydrate chains are removed by endo-b-Galactosidase digestion. Endo-b-Galactosidase-digested ZPB retains stronger spermbinding activity than ZPC. It is still unclear whether ZPA possesses significant activity. Recently, we reported that bovine sperm binds to Man 5 GlcNAc 2 , the neutral N-linked chain in the cow zona proteins. In this study, we investigated the localization of the sperm-ligand active high-mannosetype chain and the acidic complex-type chains in bovine ZPA. Three N-glycopeptides of ZPA, containing an N-glycosylation site at Asn83, Asn191 and Asn527, respectively, were obtained from endo-b-Galactosidase-digested ZPA. Of these glycosylation sites, only Asn527 is present in the ZP domain common to all the zona proteins. The carbohydrate structures of the N-linked chains obtained from each N-glycopeptide were characterized by two-dimensional sugar mapping analysis, while considering the structures of the N-linked chains of the zona protein mixture reported previously. Acidic complex-type chains were found at all three N-glycosylation sites, while Man 5 GlcNAc 2 was found at Asn83 and Asn191, but there was very little of this spermligand active chain at Asn527 in the ZP domain of ZPA.Keywords: glycoprotein; N-linked carbohydrate chain; sperm ligand; zona pellucida; ZP domain.The mammalian oocyte is coated with a transparent matrix called the zona pellucida. This matrix plays various roles in the early phase of fertilization: species-specific sperm binding, blocking polyspermy, and protecting the embryo until implantation [1,2]. The zona is composed of three glycoproteins, called ZPA, ZPB and ZPC in the order of the size of their cDNAs [3], and their carbohydrate chains are responsible for species-specific sperm-zona binding [1,4].In the pig, the carbohydrate structures of O-linked chains of zona protein mixture [5,6] and the acidic and neutral N-linked chains of ZPB/ZPC mixture [7,8] are well characterized. Sperm-binding activity has been ascribed to the O-linked chains of the zona protein mixture [9] or to the neutral N-linked chains obtained from the ZPB/ZPC mixture [8]. We have shown that the triantennary/tetraantennary chains of the ZPB/ZPC mixture possess greater activity than the diantennary chains [10]. The triantennary/ tetraantennary chains of ZPB are localized at Asn220 in the N-terminal region [10]. Moreover, the isolated N-terminal peptide of ZPB including Asn220 has sperm-binding activity [11]. Yurewicz et al. [12] showed that ZPB and ZPC form heterocomplexes that have sperm-binding activity, but that monomeric ZPB or ZPC does not exhibit this activity. These results suggest that ZPC contributes to the expression of the sperm-binding activity of the neutral N-linked chain of ZPB. In ZPC, the triantennary/tetraante...

show abstract

A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial expression and predicts a novel protein

Cited by 17 publications

References 36 publications

Protection from Pancreatitis by the Zymogen Granule Membrane Protein Integral Membrane-associated Protein-1

Protection from Pancreatitis by the Zymogen Granule Membrane Protein Integral Membrane-associated Protein-1

Effects of Muclin (Dmbt1) deficiency on the gastrointestinal system

Localization of N‐linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida

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