Catabolism of plasminogen glycoforms I and II in rabbits: Relationship to plasminogen synthesis by the rabbit liver in vitro

Hatton, M. W. C.; Southward, Suzanne M.R.; Ross-Ouellet, Bonnie

doi:10.1016/0026-0495(94)90040-x

Cited by 16 publications

(14 citation statements)

References 34 publications

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“…In the circulation, the concentration of Pg 2 is 2-fold greater than that of Pg 1 ; however, in the extravascular space the concentration of Pg 2 is almost 6-fold greater than that of Pg 1 [58]. Pg 1 contains one O-glycan at Thr-345 and one biantennary N-glycan at Asn-288, whereas Pg 2 contains only the O-glycan chain [59,60].…”

Section: Discussionmentioning

confidence: 99%

“…Pg 1 contains one O-glycan at Thr-345 and one biantennary N-glycan at Asn-288, whereas Pg 2 contains only the O-glycan chain [59,60]. Pg 1 activation is enhanced more than that of Pg 2 in the presence of fibrin by either u-PA or t-PA [61], suggesting a preferred role for Pg 1 in the intravascular space [58]. The shift in the ratio of Pg 2 to Pg 1 in the extravascular space suggests a significant role for Pg 2 glycoforms as the preferred forms for plasmin formation during metabolism on the cell surface [62].…”

Section: Discussionmentioning

confidence: 99%

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Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells

Gonzalez-Gronow¹,

Grenett²,

Weber³

et al. 2001

Biochem. J.

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Both plasminogen (Pg) activation and matrix metalloproteinases (MMPs) are involved in the proteolytic degradation of extracellular matrix components, a requisite event for malignant cell metastasis. The highly invasive 1-LN human prostate tumour cell line synthesizes and secretes large amounts of Pg activators and MMPs. We demonstrate here that the Pg type 2 (Pg 2) receptor in these cells is composed primarily of the membrane glycoprotein dipeptidyl peptidase IV (DPP IV). Pg 2 has six glycoforms that differ in their sialic acid content. Only the highly sialylated Pg 2γ, Pg 2δ and Pg 2ε glycoforms bind to DPP IV via their carbohydrate chains and induce a Ca# + signalling cascade ; Abbreviations used : ECM, extracellular matrix ; MMP, matrix metalloproteinase ; Pg, plasminogen ; DPP IV, dipeptidyl peptidase IV (CD26) ; u-PA, urinary-type plasminogen activator ; t-PA, tissue-type plasminogen activator ; mAb, monoclonal antibody ; FAPα, fibroblast activation protein α ; HBSS, Hanks balanced salt solution ; fura 2/AM, fura 2 acetoxymethyl ester ; 6-AHA, 6-aminohexanoic acid ; [Ca 2 + ] i , cytosolic free Ca 2 + concentration ; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. 1 To whom correspondence should be addressed (e-mail gonza002!mc.duke.edu). however, Pg 2ε alone is also able to significantly stimulate expression of MMP-9. We further demonstrate that the Pgmediated invasive activity of 1-LN cells is dependent on the availability of Pg 2ε. This is the first demonstration of a direct association between the expression of MMP-9 and the Pg activation system.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells

Gonzalez-Gronow¹,

Grenett²,

Weber³

et al. 2001

Biochem. J.

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“…The perfusion of rabbit livers and the analysis of the removal of radiolabeled IgG from the perfusate was done as previously reported (43).…”

Section: Materials-iodo-genmentioning

confidence: 99%

Cytokeratin 18 Is Expressed on the Hepatocyte Plasma Membrane Surface and Interacts with Thrombin-Antithrombin Complexes

Wells¹,

Hatton

Hewlett

et al. 1997

Journal of Biological Chemistry

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“…17 In previous studies, we found that Pg 2 was the preferred ligand for cellular receptors. 15,16 The concentration of Pg 2 in the extravascular space is 6-fold greater than that of Pg 1, 30 suggesting Pg 2 as the major form for Pm formation during metabolism on the cell surface. 31 However, because Pg 2 does not interfere with binding of Pg 1 to TF, our results suggest that Pm-1 may be generated even under a limited availability of this glycoform in the extravascular compartment.…”

Section: Discussionmentioning

confidence: 99%

Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells

Gonzalez-Gronow

Gawdi

Pizzo

2002

Blood

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Catabolism of plasminogen glycoforms I and II in rabbits: Relationship to plasminogen synthesis by the rabbit liver in vitro

Cited by 16 publications

References 34 publications

Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells

Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells

Cytokeratin 18 Is Expressed on the Hepatocyte Plasma Membrane Surface and Interacts with Thrombin-Antithrombin Complexes

Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells

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