Effect of protamine on the solubilization of collagen-tailed acetylcholinesterase: potential heparin-binding consensus sequences in the tail of the enzyme

Deprez, Paola; Signorelli, Janetti; Inestrosa, Nibaldo C.

doi:10.1016/0167-4838(95)00109-8

Cited by 8 publications

(9 citation statements)

References 27 publications

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“…Preparation of Rabbit Polyclonal Antibodies against Rat Recombinant MMP-7 and Its Synthetic Peptides-Two peptides of the sequences, (Cys)LRKFYLHDSKTKK (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34) and (Cys)QKLYGKRNKL (238 -247), corresponding to two putative heparin-binding sequences of rat MMP-7 in the propeptide and C-terminal region were synthesized and high pressure liquid chromatography-purified (Genemed). They were disulfide-linked to maleimide-activated keyhole limpet hemocyanin (Pierce).…”

Section: Extraction Of Mmps From Postpartum Rat Uterus-pregnantmentioning

confidence: 99%

“…5): peptide [22][23][24][25][26][27][28][29][30][31][32][33][34] (C)LRKFYLHDSKTKK and peptide 238 -247 (C)QKLYGKRNKL (Cys was added to permit coupling to hemocyanin for antibody production). The numbering of MMP-7 begins with the first residue of the propeptide (19).…”

Section: Characterization Of Putative Heparin-binding Sequences By Homentioning

confidence: 99%

“…Antibody specificities were characterized by immunoblotting (see next section). Antibodies were designated RM7-P (to propeptide [22][23][24][25][26][27][28][29][30][31][32][33][34], RM7-C (to peptide 238 -247 near the C terminus), and RM7-W (to whole recombinant rat matrilysin). RM7-W did not cross-react with human MMP-1, -2, -3, -7, -8, -9, or -13 zymogen or active forms.…”

Section: Extraction Of Mmps From Postpartum Rat Uterus-pregnantmentioning

confidence: 99%

“…The ED 50 for peptide [22][23][24][25][26][27][28][29][30][31][32][33][34] is 25 g/ml (14 M), and for peptide 238 -247 it is 165 g/ml (122 M), whereas the ED 50 for promatrilysin is 34 g/ml ( Fig. 5; 1 [22][23][24][25][26][27][28][29][30][31][32][33][34] (C)KLKDHSKYKFTLR is about 10-fold less than that of the ordered peptide.…”

Section: Characterization Of Putative Heparin-binding Sequences By Homentioning

confidence: 99%

See 3 more Smart Citations

Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)

Woessner

2000

Journal of Biological Chemistry

218

189

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Section: Extraction Of Mmps From Postpartum Rat Uterus-pregnantmentioning

confidence: 99%

Section: Characterization Of Putative Heparin-binding Sequences By Homentioning

confidence: 99%

Section: Extraction Of Mmps From Postpartum Rat Uterus-pregnantmentioning

confidence: 99%

Section: Characterization Of Putative Heparin-binding Sequences By Homentioning

confidence: 99%

See 2 more Smart Citations

Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)

Woessner

2000

Journal of Biological Chemistry

218

189

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“…Binding of highly sulfated GAGs to scavenger receptors has been reported, presumably involving an interaction with the positively charged collagen-like domain of SR-As, 29,30 but binding of less sulfated forms, such as HS and CS, has not been examined. Binding of highly sulfated GAGs has been reported to block Ox-LDL catabolism, 62 but less sulfated forms could produce other effects, such as clustering of several SR-As that bind along the same GAG chain or alteration of the conformation of the ligand-binding domain of SR-As.…”

Section: Discussionmentioning

confidence: 99%

Role of Macrophage Glycosaminoglycans in the Cellular Catabolism of Oxidized LDL by Macrophages

Kaplan

Williams

Mandel

et al. 1998

ATVB

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Abstract-Macrophage binding sites for oxidized LDL (Ox-LDL) include class A scavenger receptors (SR-As), the CD-36 molecule, and an additional but hitherto unidentified binding site. Because cell-surface glycosaminoglycans (GAGs) were previously shown to be involved in the cellular uptake of native LDL and lipoprotein(a), several strategies to assess the participation of heparan sulfate (HS) and chondroitin sulfate (CS) in macrophage catabolism of Ox-LDL were used. First, incubation of J-774 A.1 macrophage-like cells with either heparinase or chondroitinase, or with both enzymes together, reduced the binding, uptake, and degradation of 125 I-Ox-LDL by 20% to 45%, in comparison with control nontreated cells, while catabolism of 125 I-labeled acetylated LDL (Ac-LDL) and native LDL were unaffected. Second, the proteoglycan (PG) cellular content was increased by cell enrichment with exogenous GAGs or by using human monocyte-derived macrophages from two patients with Sanfilippo mucopolysaccharidosis, which are characterized by cellular HS accumulation. In these macrophages, cellular uptake of 125 I-Ox-LDL increased, while catabolism of 125 I-Ac-LDL and native LDL were unaffected. Experiments using conditioned media from control, heparinase-digested, or chondroitinase-digested macrophages indicated that neither secreted GAGs nor released digestion products played any role in Ox-LDL catabolism. To evaluate potential interactions between cell-surface GAGs and known receptors for Ox-LDL, we used excess unlabeled Ac-LDL to block SR-As or anti-CD-36 antibodies to block CD-36, and then examined the catabolism of 125 I-Ox-LDL by GAG-enriched or -depleted macrophages. Both excess unlabeled Ac-LDL and anti-CD-36 antibodies reduced 125 I-Ox-LDL catabolism, but only excess unlabeled Ac-LDL completely abolished the increase in 125 I-Ox-LDL catabolism on GAG enrichment of the cells, indicating a cooperation between exogenous GAGs and cell-surface SR-As in the catabolism of OX-LDL. Moreover, the addition of GAGases to macrophages that were preincubated with anti-CD-36 antibodies and excess Ac-LDL further reduced macrophage degradation of Ox-LDL in comparison with cells that were pretreated only with anti-CD-36 antibodies and Ac-LDL, indicating a more complex role for endogenous GAGs. Overall, these studies demonstrate a substantial contribution of macrophage-associated GAGs in the catabolism of Ox-LDL, which is mediated in part by a cooperation between GAGs and cell-surface SR-As. (Arterioscler Thromb Vasc Biol. 1998;18:542-553.) Key Words: proteoglycans Ⅲ oxidized LDL Ⅲ macrophages Ⅲ glycosaminoglycans Ⅲ mucopolysaccharidosis O xidatively modified LDL is likely to play an important contributory role in the development of atherosclerosis. Oxidized epitopes, including oxidized apoB, the major protein of Ox-LDL, have been demonstrated in human lesions. 1,2 Ox-LDL contains many biologically active molecules, such as lysophosphatidylcholine 3,4 and oxidized sterols, 5,6 that substantially alter the metabolism of arterial wall cells. Fu...

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Diversity and Processing of Acetylcholinesterase

Massoulié

Anselmet

Bon

et al. 1998

Structure and Function of Cholinesterases and Related Proteins

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Effect of protamine on the solubilization of collagen-tailed acetylcholinesterase: potential heparin-binding consensus sequences in the tail of the enzyme

Cited by 8 publications

References 27 publications

Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)

Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)

Role of Macrophage Glycosaminoglycans in the Cellular Catabolism of Oxidized LDL by Macrophages

Diversity and Processing of Acetylcholinesterase

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