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A lipocalin-derived Peptide modulating fibroblasts and extracellular matrix proteins.

Carrijo-Carvalho LC, Maria DA, Ventura JS, Morais KL, Melo RL, Rodrigues CJ, Chudzinski-Tavassi AM - J Toxicol (2012)

Bottom Line: Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar.Results indicate that modulation effects displayed by lipocalins through this sequence motif involve cell survival, extracellular matrix remodeling, and cytokine signaling.Such effects can be related to the lipocalin roles in disease, development, and tissue repair.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, Brazil.

ABSTRACT
Lipocalin family members have been implicated in development, regeneration, and pathological processes, but their roles are unclear. Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar. Lipocalins are β-barrel proteins, which have three conserved motifs in their amino acid sequence. One of these motifs was shown to be a sequence signature involved in cell modulation. The aim of this study is to investigate the effects of a synthetic peptide comprising the lipocalin sequence motif in fibroblasts. This peptide suppressed caspase 3 activity and upregulated Bcl-2 and Ki-67, but did not interfere with GPCR calcium mobilization. Fibroblast responses also involved increased expression of proinflammatory mediators. Increase of extracellular matrix proteins, such as collagen, fibronectin, and tenascin, was observed. Increase in collagen content was also observed in vivo. Results indicate that modulation effects displayed by lipocalins through this sequence motif involve cell survival, extracellular matrix remodeling, and cytokine signaling. Such effects can be related to the lipocalin roles in disease, development, and tissue repair.

No MeSH data available.


Related in: MedlinePlus

Extracellular matrix proteins in fibroblast culture. Procollagen (a), cellular fibronectin (b), and tenascin (c). Primary human fibroblasts were treated with pm2b (230 nM) and proteins were analyzed after 96 h by immunocytochemical staining (originally 400x). Data are representative images and expressed as mean ± SEM for triplicate measurements. ***P < 0.001 versus control.
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fig1: Extracellular matrix proteins in fibroblast culture. Procollagen (a), cellular fibronectin (b), and tenascin (c). Primary human fibroblasts were treated with pm2b (230 nM) and proteins were analyzed after 96 h by immunocytochemical staining (originally 400x). Data are representative images and expressed as mean ± SEM for triplicate measurements. ***P < 0.001 versus control.

Mentions: Immunofluorescence results showed that treatment with pm2b induced a significant increase of procollagen, fibronectin, and tenascin, as shown in Figure 1. In comparison to nontreated cultures, pm2b-treated fibroblasts showed almost onefold increase in tenascin (94%) and an increase in 49% of procollagen and 62% of fibronectin. Analysis of collagen type I, fibronectin, and laminin in the cell lysates by western blotting showed a significant increase in all these proteins in cultures treated with the peptide at 70 or 230 nM and a slight increase in HSP47 (Figure 2).


A lipocalin-derived Peptide modulating fibroblasts and extracellular matrix proteins.

Carrijo-Carvalho LC, Maria DA, Ventura JS, Morais KL, Melo RL, Rodrigues CJ, Chudzinski-Tavassi AM - J Toxicol (2012)

Extracellular matrix proteins in fibroblast culture. Procollagen (a), cellular fibronectin (b), and tenascin (c). Primary human fibroblasts were treated with pm2b (230 nM) and proteins were analyzed after 96 h by immunocytochemical staining (originally 400x). Data are representative images and expressed as mean ± SEM for triplicate measurements. ***P < 0.001 versus control.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3379166&req=5

fig1: Extracellular matrix proteins in fibroblast culture. Procollagen (a), cellular fibronectin (b), and tenascin (c). Primary human fibroblasts were treated with pm2b (230 nM) and proteins were analyzed after 96 h by immunocytochemical staining (originally 400x). Data are representative images and expressed as mean ± SEM for triplicate measurements. ***P < 0.001 versus control.
Mentions: Immunofluorescence results showed that treatment with pm2b induced a significant increase of procollagen, fibronectin, and tenascin, as shown in Figure 1. In comparison to nontreated cultures, pm2b-treated fibroblasts showed almost onefold increase in tenascin (94%) and an increase in 49% of procollagen and 62% of fibronectin. Analysis of collagen type I, fibronectin, and laminin in the cell lysates by western blotting showed a significant increase in all these proteins in cultures treated with the peptide at 70 or 230 nM and a slight increase in HSP47 (Figure 2).

Bottom Line: Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar.Results indicate that modulation effects displayed by lipocalins through this sequence motif involve cell survival, extracellular matrix remodeling, and cytokine signaling.Such effects can be related to the lipocalin roles in disease, development, and tissue repair.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, Brazil.

ABSTRACT
Lipocalin family members have been implicated in development, regeneration, and pathological processes, but their roles are unclear. Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar. Lipocalins are β-barrel proteins, which have three conserved motifs in their amino acid sequence. One of these motifs was shown to be a sequence signature involved in cell modulation. The aim of this study is to investigate the effects of a synthetic peptide comprising the lipocalin sequence motif in fibroblasts. This peptide suppressed caspase 3 activity and upregulated Bcl-2 and Ki-67, but did not interfere with GPCR calcium mobilization. Fibroblast responses also involved increased expression of proinflammatory mediators. Increase of extracellular matrix proteins, such as collagen, fibronectin, and tenascin, was observed. Increase in collagen content was also observed in vivo. Results indicate that modulation effects displayed by lipocalins through this sequence motif involve cell survival, extracellular matrix remodeling, and cytokine signaling. Such effects can be related to the lipocalin roles in disease, development, and tissue repair.

No MeSH data available.


Related in: MedlinePlus