PMID- 10103056
OWN - NLM
STAT- MEDLINE
DCOM- 19990519
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 261
IP  - 1
DP  - 1999 Apr
TI  - Cloning and structural analysis of leydin, a novel human serine protease
      expressed by the Leydig cells of the testis.
PG  - 244-50
AB  - We present the cloning and structural analysis of a novel member of the large
      family of trypsin-related serine proteases. Northern blot analysis shows that
      this protease, in adult tissues, is expressed almost exclusively in the human
      testis. In addition, a larger transcript was detected in relatively high
      abundance in several embryonic tissues, indicating different functions during
      embryonic and adult life. Sera raised against this protease was used to locate
      the expression in adult tissues to the testosterone producing cells of the
      testis, the interstitial Leydig cells. We therefore propose the name leydin for
      this novel protease. Leydin is clearly distinct from acrosin, the other
      testis-specific serine protease which is expressed by the spermatocytes. Leydin
      is probably a two-chain protease such as acrosin, prostasin, and coagulation
      factor XI. The heavy chain consists of 246 amino acids, corresponding to a
      molecular mass of 27384 Da and a net charge of +10.76. The size of the light
      chain is between 9 and 18 amino acids depending on the site of proteolytic
      cleavage, which remains to be determined. The amino-acid residues surrounding the
      active site indicate a trypsin-like cleavage specificity. The presence of two
      dibasic sequences Arg-Arg and Lys-Arg at the N-terminus of the heavy chain
      indicate that one or more subtilisin-like endopeptidases are responsible for the 
      processing of leydin. However, leydin may also be activated by a trypsin-like
      enzyme, possibly by auto catalysis.
FAU - Poorafshar, M
AU  - Poorafshar M
AD  - Department of Cell and Molecular Biology, University of Uppsala, Biomedical
      Center, Uppsala, Sweden.
FAU - Hellman, L
AU  - Hellman L
LA  - eng
SI  - GENBANK/AF077298
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.- (leydin)
SB  - IM
MH  - Adult
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - Dimerization
MH  - Gene Expression
MH  - Humans
MH  - Immunohistochemistry
MH  - Leydig Cells/*enzymology
MH  - Male
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Phylogeny
MH  - Protein Conformation
MH  - RNA, Messenger/genetics/metabolism
MH  - Serine Endopeptidases/*chemistry/*genetics/metabolism
MH  - Tissue Distribution
EDAT- 1999/04/02 00:00
MHDA- 1999/04/02 00:01
CRDT- 1999/04/02 00:00
PHST- 1999/04/02 00:00 [pubmed]
PHST- 1999/04/02 00:01 [medline]
PHST- 1999/04/02 00:00 [entrez]
AID - 10.1046/j.1432-1327.1999.00266.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1999 Apr;261(1):244-50. doi: 10.1046/j.1432-1327.1999.00266.x.