The platelet receptor for type III collagen (TIIICBP) is present in platelet membrane lipid microdomains (rafts)

Maurice, Pascal; Waeckel, Ludovic; Pires, Viviane Silva; Sonnet, Pascal; Lemesle, Monique; Arbeille, B.; Vassy, Jany; Rochette, Jacques; Legrand, Chantal; Fauvel-Lafève, Françoise

doi:10.1007/s00418-005-0076-y

Cited by 17 publications

(10 citation statements)

References 45 publications

(68 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Several platelet receptors for collagen have been described, and a new receptor for type III collagen, named TIIICBP for Type III Collagen Binding Protein, speciWcally recognizes an octapeptide sequence from human type III collagen. In continuation of their earlier studies, Maurice et al (2006) show by electron microscopy that in resting platelets TIIICBP is present on the platelet membrane and associated with the open canalicular system, then redistributes to the platelet membrane upon platelet activation. TIIICBP could be recovered in lipid raft-containing fractions and Triton X-100 insoluble fractions enriched in cytoskeleton proteins.…”

Section: Aspects Of Cell Membranes: Caveolins Transporters Junctionmentioning

confidence: 67%

The histochemistry and cell biology vade mecum: a review of 2005–2006

Taatjes

Zuber

Roth

2006

Histochem Cell Biol

View full text Add to dashboard Cite

The procurement of new knowledge and understanding in the ever expanding discipline of cell biology continues to advance at a breakneck pace. The progress in discerning the physiology of cells and tissues in health and disease has been driven to a large extent by the continued development of new probes and imaging techniques. The recent introduction of semi-conductor quantum dots as stable, specific markers for both fluorescence light microscopy and electron microscopy, as well as a virtual treasure-trove of new fluorescent proteins, has in conjunction with newly introduced spectral imaging systems, opened vistas into the seemingly unlimited possibilities for experimental design. Although it oftentimes proves difficult to predict what the future will hold with respect to advances in disciplines such as cell biology and histochemistry, it is facile to look back on what has already occurred. In this spirit, this review will highlight some advancements made in these areas in the past 2 years.

show abstract

Section: Aspects Of Cell Membranes: Caveolins Transporters Junctionmentioning

confidence: 67%

The histochemistry and cell biology vade mecum: a review of 2005–2006

Taatjes

Zuber

Roth

2006

Histochem Cell Biol

View full text Add to dashboard Cite

show abstract

“…A new receptor for type III collagen, named TIIICBP, speciWcally recognizes an octapeptide sequence from human type III collagen. In continuation of their earlier studies, Maurice et al (2006) show that in resting platelets TIIICBP is present on the platelet membrane and associated with the open canalicular system, and redistributes to the platelet membrane upon platelet activation. TIIICBP could be recovered in lipid raft-containing fractions and Triton X-100 insoluble fractions enriched in cytoskeletal proteins.…”

Section: Aspects Of Cell Membranes: Channels Caveolins Junctional Pmentioning

confidence: 71%

Recent progress in histochemistry

Zuber

Taatjes

Roth

2007

Histochem Cell Biol

View full text Add to dashboard Cite

show abstract

“…While this suggests that direct localization of IGFBP‐3 to lipid rafts is possible, it is also possible that ECM‐bound molecules might also localize to the TIS fraction. For example, β1‐integrins interact with a number of ECM proteins and the platelet receptor for type III collagen has been localized to lipid rafts (Maurice et al, 2006). Identification of the specific pH‐dependent binding partner is needed to conclude more.…”

Section: Discussionmentioning

confidence: 99%

Enhanced insulin‐like growth factor‐I (IGF‐I) cell association at reduced pH is dependent on IGF binding protein‐3 (IGFBP‐3) interaction

Forsten-Williams

Cassino

Delo

et al. 2006

Journal Cellular Physiology

View full text Add to dashboard Cite

The cellular microenvironment impacts how signals are transduced by cells and plays a key role in tissue homeostasis. Although pH is generally well regulated, there are a number of situations where acidosis occurs and our work addresses how low pH impacts cell association of insulin-like growth factor-I (IGF-I) in the presence of IGF binding protein-3 (IGFBP-3). We have previously shown that IGF-I cell binding was enhanced in the presence of IGFBP-3 at low pH and now show that this binding is IGFBP-mediated as it is inhibited by Y60L-IGF-I, a mutant with reduced affinity for the IGF receptor (IGF-IR), and unaffected by insulin, which binds but not IGFBPs. Using surface plasmon resonance (SPR), we show that direct binding between IGF-I and IGFBP-3 is pH sensitive. Despite this, the key step in the process appears to be IGFBP-3 cell surface association as Long-R(3)-IGF-I, a mutant with reduced affinity for IGFBPs, shows a similar increase in cell association at pH 5.8 in the presence of IGFBP-3 but does not exhibit pH-dependent binding by SPR. Further, analysis indicates a large increase in low-affinity binding sites for IGF-I in the presence of IGFBP-3 and an elimination of IGF-I enhanced binding when a non-cell associating mutant of IGFBP-3 is added in place of IGFBP-3. That the IGFBP-3-mediated binding localizes IGF-I away from IGF-IR is suggested by triton-solubility testing and indicates additional complexities to IGF-I regulation by IGFBP-3. Identifying the pH-dependent binding partner(s) for IGFBP-3 is a necessary next step in deciphering this process.

show abstract

The platelet receptor for type III collagen (TIIICBP) is present in platelet membrane lipid microdomains (rafts)

Cited by 17 publications

References 45 publications

The histochemistry and cell biology vade mecum: a review of 2005–2006

The histochemistry and cell biology vade mecum: a review of 2005–2006

Recent progress in histochemistry

Enhanced insulin‐like growth factor‐I (IGF‐I) cell association at reduced pH is dependent on IGF binding protein‐3 (IGFBP‐3) interaction

Contact Info

Product

Resources

About