PubMed Journals: Proc Natl Acad Sci U S A
Source: PMID: 3927292
⇦ ⇨ Proc Natl Acad Sci U S A. 1985 Aug;82(15):4910-4.
Cloning and sequence analysis of cDNA for
human cathepsin D.
Faust PL, Kornfeld S, Chirgwin JM.
An 1110-base-pair cDNA clone for human cathepsin
D was obtained by screening a lambda gt10
human hepatoma G2 cDNA library with a human
renin exon 3 genomic fragment. Poly(A)+
RNA blot analysis with this cathepsin D
clone demonstrated a message length of about
2.2 kilobases. The partial clone was used
to screen a size-selected human kidney cDNA
library, from which two cathepsin D recombinant
plasmids with inserts of about 2200 and
2150 base pairs were obtained. The nucleotide
sequences of these clones and of the lambda
gt10 clone were determined. The amino acid
sequence predicted from the cDNA sequence
shows that human cathepsin D consists of
412 amino acids with 20 and 44 amino acids
in a pre- and a prosegment, respectively.
The mature protein region shows 87% amino
acid identity with porcine cathepsin D but
differs in having nine additional amino
acids. Two of these are at the COOH terminus;
the other seven are positioned between the
previously determined junction for the light
and heavy chains of porcine cathepsin D.
A high degree of sequence homology was observed
between human cathepsin D and other aspartyl
proteases, suggesting a conservation of
three-dimensional structure in this family
PMCID: PMC390467 PMID: 3927292 [Indexed