Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.24.3 (
collagenase
)
18,340
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Surfactant protein D
(
SP-D
) is a member of the C-type lectin superfamily with four distinct structural domains: an amino terminus involved in forming intermolecular disulfides, a collagen-like domain, a neck region, and a carbohydrate recognition domain. A collagen domain deletion mutant (CDM) of
SP-D
was created by site-directed mutagenesis. A second variant lacking both the amino-terminal region and the collagen-like domain was generated by
collagenase
treatment and purification of the
collagenase
-resistant fragment (CRF). The CDM expressed in CHO-K1 cells formed the covalent trimers, but not the noncovalent dodecamers, typical of native
SP-D
. The CRF derived from recombinant
SP-D
formed only monomers. The CDM bound mannose-Sepharose and phosphatidylinositol (PI) as well as
SP-D
, but the binding to mannosyl bovine serum albumin and glucosylceramide was diminished by approximately 60%. The CRF displayed weak binding to mannose-Sepharose and PI and essentially no binding to mannosyl bovine serum albumin and glucosylceramide. Both
SP-D
and CDM altered the self-aggregation of PI-containing liposomes.
SP-D
reduced the density and the light scattering properties of PI aggregates. These results demonstrate that the collagen-like domain is required for dodecamer but not covalent trimer formation of
SP-D
and plays an important, but not essential, role in the interaction of
SP-D
with PI and GlcCer. Removal of the amino-terminal domain of
SP-D
along with the collagen-like domain diminishes PI binding and effectively eliminates GlcCer binding.
...
PMID:The role of the amino-terminal domain and the collagenous region in the structure and the function of rat surfactant protein D. 764 68
Surfactant protein D
(
SP-D
) is a collectin believed to play an important role in innate immunity.
SP-D
is characterized by having a collagen-like domain and a carbohydrate recognition domain (CRD), which has a specific Ca(2+)-dependent specificity for saccharides and thus the ability to bind complex glycoconjugates on micro-organisms. This paper describes the tissue immunolocalization of porcine
SP-D
(pSP-D) in normal slaughter pigs using a monoclonal antibody raised against purified pSP-D. Porcine
SP-D
was purified from porcine bronchoalveolar lavage (BAL) by maltose-agarose and immunoglobulin M affinity chromatography. The purified protein appeared on sodium dodecyl sulphate-polyacrylamide gel electrophoresis as a band of approximately 53,000 MW in the reduced state and approximately 138,000 MW in the unreduced state. Porcine
SP-D
was sensitive to
collagenase
digestion and N-deglycosylation, which reduced the molecular mass to approximately 24,000 MW and approximately 48,000 MW respectively, in the reduced state. N-deglycosylation of the collagen-resistant fragment, reduced the molecular mass to approximately 21,000 MW showing the presence of an N-glycosylation site located in the CRD. Porcine
SP-D
bound to solid-phase mannan in a dose and Ca(2+)-dependent manner with a saccharide specificity similar to rat and human
SP-D
. The purified protein was used for the production of a monoclonal anti-pSP-D antibody. The antibody reacted specifically with pSP-D in the reduced and unreduced state when analysed by Western blotting. Immunohistochemical evaluation of normal porcine tissues showed pSP-D immunoreactivity predominantly in Clara cells and serous cells of the bronchial submucosal glands, and to a lesser extent in alveolar type II cells, epithelial cells of the intestinal glands (crypts of Lieberkuhn) in the duodenum, jejunum and ileum and serous cells of the dorsolateral lacrimal gland.
...
PMID:Purification, characterization and immunolocalization of porcine surfactant protein D. 1560 97
