HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Furukawa, M. Articles by Hirose, S. Search for Related Content PubMed PubMed Citation Articles by Furukawa, M. Articles by Hirose, S. Social Bookmarking                      What's this?

Volume 271, Number 47, Issue of November 22, 1996 pp. 29517-29520
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

---

COMMUNICATION:
Cryptic Origin of SPAI, a Plasma Protein with a Transglutaminase Substrate Domain and the WAP Motif, Revealed by in Situ Hybridization and Immunohistochemistry

(Received for publication, August 28, 1996, and in revised form, October 1, 1996)

From the Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226, Japan and the ^§ Tsukuba Research Laboratories, Eisai Co., Ltd., Tsukuba 300-26, Japan

SPAI, originally isolated as a odium/otassium-TPase nhibitor and now considered to be a proteinase inhibitor of unknown specificity based on its similarity to elafin (an elastase inhibitor), is a new type of plasma protein that has a transglutaminase substrate domain, which serves as an anchoring sequence to be covalently cross-linked at target sites. To determine the source of SPAI, we carried out in situ hybridization and immunohistochemistry using an antisense cRNA probe and an antiserum against recombinant SPAI, respectively. Since previous RNase protection analysis had indicated that SPAI mRNA is almost exclusively expressed in the porcine small intestine, we used its frozen sections for the staining. The lower crypt was decorated with both the cRNA probe and antiserum, indicating that SPAI is synthesized and secreted by the enteroendocrine cells located near the crypt base. The native form of SPAI was also characterized by Western blotting. This result together with the previous biochemical and molecular biological characterizations may set the stage for identifying the physiological roles of the conceptually very interesting protein SPAI.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				Y. Furutani, A. Kato, A. Fibriani, T. Hirata, R. Kawai, J.-H. Jeon, Y. Fujii, I.-G. Kim, S. Kojima, and S. Hirose Identification, Evolution, and Regulation of Expression of Guinea Pig Trappin with an Unusually Long Transglutaminase Substrate Domain J. Biol. Chem., May 27, 2005; 280(21): 20204 - 20215. [Abstract] [Full Text] [PDF]

				A. M. Torres, H. Y. Wong, M. Desai, S. Moochhala, P. W. Kuchel, and R. M. Kini Identification of a Novel Family of Proteins in Snake Venoms: PURIFICATION AND STRUCTURAL CHARACTERIZATION OF NAWAPRIN FROM NAJA NIGRICOLLIS SNAKE VENOM J. Biol. Chem., October 10, 2003; 278(41): 40097 - 40104. [Abstract] [Full Text] [PDF]