1: Gene. 2001 Sep 5;275(1):93-101. 

Cloning and characterization of human cathepsin L promoter.

Bakhshi R, Goel A, Seth P, Chhikara P, Chauhan SS.

Department of Biochemistry, All India Institute of Medical Sciences, New Delhi
110029, India.

Cathepsin L is a lysosomal cysteine protease, which is over-expressed and
secreted by malignant cells. It is very potent in degrading collagen, elastin,
laminin and other components of the basement membrane and, therefore, has been
implicated in tumor invasion and metastasis. The structural portion of the human
cathepsin L (hCATL) gene was cloned to elucidate its genomic organization
(Chauhan et al., J. Biol. Chem. 218 (1993) 1039). In the present study, a 1.90
kb DNA fragment, containing 1825 bp of the 5' upstream region of hCATL and 75
bases of the first exon of the hCATL, was amplified by PCR from an adaptor
ligated placental genomic library. This fragment has been demonstrated to
exhibit promoter activity by luciferase reporter assays. Sequence analysis of
this fragment revealed the presence of approximately 29 different putative
transcription factor binding sites. Several of them like AP-4, GATA-1, Lmo2,
CEBPB, MZF-1, NF-AT, etc. were present more than once in this region. However, a
consensus CAAT box but no consensus TATA box was found within the 1.0 kb
upstream of exon 1. The transcription initiation site of hCATL, using placental
total RNA, was mapped to a single adenine residue 289 bases upstream of the ATG
codon.

PMID: 11574156 [PubMed - indexed for MEDLINE]


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