NDLI: Phosphoenolpyruvate-dependent inhibition of collagen biosynthesis, α$_{2}$β$_{1}$ integrin and IGF-I receptor signaling in cultured fibroblasts

Content Provider	Springer Nature Link
Author	Karna, Ewa Palka, Jerzy A.
Copyright Year	2008
Abstract	The mechanism of collagen biosynthesis regulation is not fully understood. The finding that prolidase plays an important role in collagen biosynthesis and phosphoenolpyruvate inhibits prolidase activity “in vitro” led to evaluate its effect on collagen biosynthesis in cultured human skin fibroblasts. Confluent fibroblasts were treated with millimolar concentrations (1–4 mM) of phosphoenolpyruvate monopotassium salt (PEP) for 24 h. It was found that PEP-dependent decrease in prolidase activity and expression was accompanied by parallel decrease in collagen biosynthesis. However, the experiments with inhibitor of PEP production, 3-mercaptopicolinate revealed no direct correlation between collagen biosynthesis and prolidase activity and expression. Since insulin-like growth factor (IGF-I) is the most potent stimulator of both collagen biosynthesis and prolidase activity, and prolidase is regulated by β$_{1}$ integrin signaling, the effect of PEP on IGF-I receptor (IGF-IR) and β$_{1}$ integrin receptor expressions were evaluated. It was found that the exposure of the cells to 4 mM PEP contributed to a decrease in IGF-IR and β$_{1}$ integrin receptor expressions. The data suggest that PEP-dependent decrease of collagen biosynthesis in cultured human skin fibroblasts may undergo through depression of α$_{2}$β$_{1}$ integrin and IGF-IR signaling. The hypothetical mechanism of the role of prolidase in IGF-IR, β$_{1}$ integrin receptor expressions, and clinical significance of the process are discussed.
Starting Page	61
Ending Page	67
Page Count	7
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	315
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Springer US
Publisher Date	2008-05-21
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	α$_{2}$β$_{1}$ Integrin receptor Collagen biosynthesis Fibroblasts IGF-I receptor Phosphoenolpyruvate Prolidase Cardiology Oncology Medical Biochemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Butyrate-induced collagen biosynthesis in cultured fibroblasts is independent on α$_{2}$β$_{1}$ integrin signalling and undergoes through IGF-I receptor cascade

Protective effect of hyaluronic acid on interleukin-1-induced deregulation of β$_{1}$-integrin and insulin-like growth factor-I receptor signaling and collagen biosynthesis in cultured human chondrocytes

The mechanism of oxythiamine-induced collagen biosynthesis in cultured fibroblasts

Short communication oxidative stress induces igf-i receptor signaling disturbances in cultured human dermal fibroblasts. A possible mechanism for collagen biosynthesis inhibition (2004).

Insulin-like growth factor I-dependent regulation of prolidase activity in cultured human skin fibroblasts

Thrombin-dependent modulation of β$_{1}$-integrin-mediated signaling up-regulates prolidase and HIF-1α through p-FAK in colorectal cancer cells

Collagen binding α$_{2}$β$_{1}$ and α$_{1}$β$_{1}$ integrins play contrasting roles in regulation of Ets-1 expression in human liver myofibroblasts

Oxidative stress induces IGF-I receptor signaling disturbances in cultured human dermal fibroblasts. A possible mechanism for collagen biosynthesis inhibition.

The mechanism of oxythiamine-induced collagen biosynthesis in cultured fibroblasts

Phosphoenolpyruvate-dependent inhibition of collagen biosynthesis, α$_{2}$β$_{1}$ integrin and IGF-I receptor signaling in cultured fibroblasts

Similar Documents

Butyrate-induced collagen biosynthesis in cultured fibroblasts is independent on α$_{2}$β$_{1}$ integrin signalling and undergoes through IGF-I receptor cascade

Protective effect of hyaluronic acid on interleukin-1-induced deregulation of β$_{1}$-integrin and insulin-like growth factor-I receptor signaling and collagen biosynthesis in cultured human chondrocytes

The mechanism of oxythiamine-induced collagen biosynthesis in cultured fibroblasts

Short communication oxidative stress induces igf-i receptor signaling disturbances in cultured human dermal fibroblasts. A possible mechanism for collagen biosynthesis inhibition (2004).

Insulin-like growth factor I-dependent regulation of prolidase activity in cultured human skin fibroblasts

Thrombin-dependent modulation of β$_{1}$-integrin-mediated signaling up-regulates prolidase and HIF-1α through p-FAK in colorectal cancer cells

Collagen binding α$_{2}$β$_{1}$ and α$_{1}$β$_{1}$ integrins play contrasting roles in regulation of Ets-1 expression in human liver myofibroblasts

Oxidative stress induces IGF-I receptor signaling disturbances in cultured human dermal fibroblasts. A possible mechanism for collagen biosynthesis inhibition.

The mechanism of oxythiamine-induced collagen biosynthesis in cultured fibroblasts

Phosphoenolpyruvate-dependent inhibition of collagen biosynthesis, α$_{2}$β$_{1}$ integrin and IGF-I receptor signaling in cultured fibroblasts