Top-down HPLC-ESI-MS characterization of rat gliadoralin A, a new member of the family of rat submandibular gland glutamine-rich proteins and potential substrate of transglutaminase

2013 ◽  
Vol 36 (17) ◽  
pp. 2848-2861 ◽  
Author(s):  
Tiziana Cabras ◽  
Federica Iavarone ◽  
Davide Pirolli ◽  
Maria Cristina De Rosa ◽  
Alberto Vitali ◽  
...  
Keyword(s):  
Submandibular Gland ◽  
Top Down ◽  
Esi Ms ◽  
The Family ◽  
Rat Submandibular Gland ◽  
Potential Substrate

scholarly journals Immunohistochemical localization of rat submandibular gland esterase B (homologous to the RSKG-7 kallikrein gene) in relation to other serine proteases of the kallikrein family.

1992 ◽  
Vol 40 (1) ◽  
pp. 83-92 ◽  
Author(s):  
T Berg ◽  
I Wassdal ◽  
K Sletten
Keyword(s):  
Submandibular Gland ◽  
Serine Proteases ◽  
Cross Reactivity ◽  
Immunohistochemical Localization ◽  
Staining Reaction ◽  
Anatomic Distribution ◽  
Family Gene ◽  
Terminal Amino ◽  
Rat Submandibular Gland

The rat submandibular gland contains several members of the kallikrein family. In the present study we purified and raised an antiserum against one of these enzymes, i.e., esterase B, which was first described by Khullar et al. in 1986. N-terminal amino acid analysis revealed complete homology between esterase B and the kallikrein family gene RSKG-7. For characterization of the antiserum, flat-bed isoelectrofocusing with immunoblotting was superior to immunoelectrophoresis and double immunodiffusion in detecting and identifying crossreacting proteins. This was due to the fact that kallikrein-like enzymes were readily separated by isoelectrofocusing, and immunoreactivity was easily detected by the sensitive peroxidase-anti-peroxidase staining after blotting onto nitrocellulose membrane. Immunohistochemical controls were carried out accordingly, including homologous as well as crossreacting antigens. In the submandibular gland, esterase B was detected exclusively in all granular convoluted tubular cells, co-localized with tissue kallikrein and tonin. Some staining was also observed in striated duct cells; however, this staining reaction was induced by cross-reactivity with kallikrein, since staining was abolished by addition of kallikrein as well as esterase B to the primary antiserum. It was therefore concluded that like tonin and antigen gamma, but unlike kallikrein, esterase B was not detected in the striated ducts of the submandibular, parotid, or sublingual glands. This separation in anatomic distribution between esterase B and kallikrein may indicate that prokallikrein activation is not the only biological function of esterase B.

Molecular cloning and characterization of the gene encoding rat submandibular gland apomucin,Mucsmg

1996 ◽  
Vol 13 (5) ◽  
pp. 709-716 ◽  
Author(s):  
Earl F. Albone ◽  
Fred K. Hagen ◽  
Claude Szpirer ◽  
Lawrence A. Tabak
Keyword(s):  
Molecular Cloning ◽  
Submandibular Gland ◽  
Gene Encoding ◽  
Rat Submandibular Gland

Molecular Cloning of Developmentally Regulated Neonatal Rat Submandibular Gland Proteins

1993 ◽  
Vol 4 (3) ◽  
pp. 525-530 ◽  
Author(s):  
Lily Mirels ◽  
Lisa R. Girard ◽  
William D. Ball
Keyword(s):  
Molecular Cloning ◽  
Submandibular Gland ◽  
Cdna Library ◽  
Protein C ◽  
Salivary Protein ◽  
Neonatal Rat ◽  
Salivary Proteins ◽  
Developmentally Regulated ◽  
Rat Submandibular Gland

At birth, the rat submandibular gland (SMG) contains two transient secretory cell types that produce several characteristic salivary proteins. Proteins SMG-A, B1, and B2 (23.5, 26 and 27.5 kDa) are products of the neonatal type III cells, but not the adult acinar cells. Protein C (89 kDa), a major product of the neonatal type I cells, is either absent or present at greatly diminished levels in the secretory cells of the adult gland. The decrease in biosynthesis of these neonatal salivary proteins occurs concomitantly with the increase in levels of characteristic adult SMG products. In order to understand these developmentally regulated changes in SMG salivary protein gene expression, we have initiated the molecular cloning and characterization of neonatal submandibular gland proteins from a 5-d-old rat submandibular gland cDNA library. Clones encoding SMG-A were isolated by homology to the mouse parotid secretory protein (PSP). SMG-A was shown to be derived from a salivary protein multigene family that also includes PSP. Cloning and characterization of additional neonatal rat submandibular gland proteins was initiated by screening the 5-d-old rat submandibular gland cDNA library with first strand cDNA prepared from 1-d-old rat submandibular glands. Clones corresponding to a highly abundant 3 kb transcript present in the neonatal rat SMG, but not in adult submandibular, sublingual, or parotid gland have been identified. The size, abundance, and organ specificity of this transcript suggest that it may encode protein C. One clone derived from an unknown transcript that is developmentally regulated in the neonatal SMG and is present in the adult parotid, submandibular, and sublingual glands was also identified.

scholarly journals A Mini Review on Capillary Isoelectric Focusing-Mass Spectrometry for Top-Down Proteomics

2021 ◽  
Vol 9 ◽  
Author(s):  
Tian Xu ◽  
Liangliang Sun
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Isoelectric Focusing ◽  
Large Scale ◽  
Protein Characterization ◽  
Capillary Isoelectric Focusing ◽  
Top Down ◽  
Esi Ms ◽  
Highly Sensitive

Mass spectrometry (MS)-based top-down proteomics (TDP) requires high-resolution separation of proteoforms before electrospray ionization (ESI)-MS and tandem mass spectrometry (MS/MS). Capillary isoelectric focusing (cIEF)-ESI-MS and MS/MS could be an ideal method for TDP because cIEF can enable separation of proteoforms based on their isoelectric points (pIs) with ultra-high resolution. cIEF-ESI-MS has been well-recognized for protein characterization since 1990s. However, the widespread adoption of cIEF-MS for the characterization of proteoforms had been impeded by several technical challenges, including the lack of highly sensitive and robust ESI interface for coupling cIEF to MS, ESI suppression of analytes from ampholytes, and the requirement of manual operations. In this mini review, we summarize the technical improvements of cIEF-ESI-MS for characterizing proteoforms and highlight some recent applications to hydrophobic proteins, urinary albumin variants, charge variants of monoclonal antibodies, and large-scale TDP of complex proteomes.

Characterization of nontransformed and transformed androgen receptor from rat submandibular gland

1985 ◽  
Vol 839 (3) ◽  
pp. 249-257 ◽  
Author(s):  
Takayuki Nemoto ◽  
Yuko Ohara-Nemoto ◽  
Nobuko Sato ◽  
Seiko Kyakumoto ◽  
Minoru Ota
Keyword(s):  
Androgen Receptor ◽  
Submandibular Gland ◽  
Rat Submandibular Gland

Establishment and characterization of an epithelial cell line from the rat submandibular gland

1989 ◽  
Vol 18 (4) ◽  
pp. 206-213 ◽  
Author(s):  
Ashley M. Brown ◽  
Eileen J. Rusnock ◽  
James J. Sciubba ◽  
Bruce J. Baum
Keyword(s):  
Epithelial Cell ◽  
Cell Line ◽  
Submandibular Gland ◽  
Epithelial Cell Line ◽  
Rat Submandibular Gland

Characterization of microsomal long-chain acyl-CoA hydrolase activity in the rat submandibular gland

1994 ◽  
Vol 26 (2) ◽  
pp. 279-285 ◽  
Author(s):  
Shin Sun-Ok ◽  
Kameyama Yasunaga ◽  
Yoshida Masamichi ◽  
Takatsu Fuyuakira ◽  
Shinkai Akira ◽  
...  
Keyword(s):  
Submandibular Gland ◽  
Hydrolase Activity ◽  
Chain Acyl ◽  
Coa Hydrolase ◽  
Rat Submandibular Gland ◽  
Long Chain
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