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Endocrinology Vol. 141, No. 6 2033-2042
Copyright © 2000 by The Endocrine Society


ARTICLES

Identification of ADAM 31: A Protein Expressed in Leydig Cells and Specialized Epithelia1

Limin Liu and Jeffrey W. Smith

Program on Cell Adhesion at the Cancer Research Center, The Burnham Institute, La Jolla, California 92037

Address all correspondence and requests for reprints to: Dr. Jeffrey W. Smith, Program on Cell Adhesion at the Cancer Research Center, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037. E-mail: jsmith{at}burnham-inst.org

A family of proteins containing a disintegrin and metalloproteinase domain (ADAMs) has been identified recently. Here, we report the identification of a novel member of the ADAM protein family from mouse. This protein is designated ADAM 31. The complementary DNA sequence of ADAM 31 predicts a transmembrane protein with metalloproteinase, disintegrin, cysteine-rich, and cytoplasmic domains. Messenger RNA encoding ADAM 31 was most abundant in testes, but was also detected in many other tissues. More significantly, the antibodies raised against ADAM 31 reveal that the protein has a unique and restricted expression pattern. ADAM 31 is expressed in Leydig cells of the testes, but unlike many other ADAMs, it is not found on developing sperm. Furthermore, ADAM 31 is highly expressed on four types of specialized epithelia: the cauda epididymidis, the vas deferens, the convoluted tubules of the kidney, and the parietal cells of the stomach.




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S. Mazaud Guittot, A. Verot, F. Odet, M.-A. Chauvin, and B. le Magueresse-Battistoni
A comprehensive survey of the laminins and collagens type IV expressed in mouse Leydig cells and their regulation by LH/hCG
Reproduction, April 1, 2008; 135(4): 479 - 488.
[Abstract] [Full Text] [PDF]




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