Abstract
Disorders of wound healing characterized by impaired or delayed re-epithelialization are a serious medical problem. These conditions affect many tissues, are painful, and are difficult to treat. In this study, using cornea as a model, we demonstrate for the first time the importance of carbohydrate-binding proteins galectins-3 and -7 in re-epithelialization of wounds. In two different models of corneal wound healing, re-epithelialization of wounds was significantly slower in galectin-3-deficient (gal3-/-) mice compared with wild-type (gal3+/+) mice. In contrast, there was no difference in corneal epithelial wound closure rates between galectin-l-deficient and wild-type mice. Quantitation of the bromodeoxyuridine-labeled cells in gal3+/+ and gal3-/- corneas revealed that corneal epithelial cell proliferation rate is not perturbed in gal3-/- corneas. Exogenous galectin-3 accelerated re-epithelialization of wounds in gal3+/+ mice but, surprisingly, not in the gal3-/- mice. Gene expression analysis using cDNA microarrays revealed that healing corneas of gal3-/- mice contain markedly reduced levels of galectin-7 compared with those of gal3+/+ mice. More importantly, unlike galectin-3, galectin-7 accelerated re-epithelialization of wounds in both gal3-/- and gal3+/+ mice. In corresponding experiments, recombinant galectin-1 did not stimulate the corneal epithelial wound closure rate. The extent of acceleration of re-epithelialization of wounds with both galectin-3 and galectin-7 was greater than that observed in most of the published studies using growth factors. These findings have broad implications for developing novel therapeutic strategies for treating nonhealing wounds.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 42299-42305 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 277 |
| Issue number | 44 |
| DOIs | |
| State | Published - Nov 1 2002 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Galectins-3 and -7, but not galectin-1, play a role in re-epithelialization of wounds. / Cao, Zhiyi; Said, Neveen; Amin, Shalin; Wu, Helen K.; Bruce, Amenda; Garate, Marco; Hsu, Daniel K.; Kuwabara, Ichiro; Liu, Fu-Tong; Panjwani, Noorjahan.
In: Journal of Biological Chemistry, Vol. 277, No. 44, 01.11.2002, p. 42299-42305.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Galectins-3 and -7, but not galectin-1, play a role in re-epithelialization of wounds
AU - Cao, Zhiyi
AU - Said, Neveen
AU - Amin, Shalin
AU - Wu, Helen K.
AU - Bruce, Amenda
AU - Garate, Marco
AU - Hsu, Daniel K.
AU - Kuwabara, Ichiro
AU - Liu, Fu-Tong
AU - Panjwani, Noorjahan
PY - 2002/11/1
Y1 - 2002/11/1
N2 - Disorders of wound healing characterized by impaired or delayed re-epithelialization are a serious medical problem. These conditions affect many tissues, are painful, and are difficult to treat. In this study, using cornea as a model, we demonstrate for the first time the importance of carbohydrate-binding proteins galectins-3 and -7 in re-epithelialization of wounds. In two different models of corneal wound healing, re-epithelialization of wounds was significantly slower in galectin-3-deficient (gal3-/-) mice compared with wild-type (gal3+/+) mice. In contrast, there was no difference in corneal epithelial wound closure rates between galectin-l-deficient and wild-type mice. Quantitation of the bromodeoxyuridine-labeled cells in gal3+/+ and gal3-/- corneas revealed that corneal epithelial cell proliferation rate is not perturbed in gal3-/- corneas. Exogenous galectin-3 accelerated re-epithelialization of wounds in gal3+/+ mice but, surprisingly, not in the gal3-/- mice. Gene expression analysis using cDNA microarrays revealed that healing corneas of gal3-/- mice contain markedly reduced levels of galectin-7 compared with those of gal3+/+ mice. More importantly, unlike galectin-3, galectin-7 accelerated re-epithelialization of wounds in both gal3-/- and gal3+/+ mice. In corresponding experiments, recombinant galectin-1 did not stimulate the corneal epithelial wound closure rate. The extent of acceleration of re-epithelialization of wounds with both galectin-3 and galectin-7 was greater than that observed in most of the published studies using growth factors. These findings have broad implications for developing novel therapeutic strategies for treating nonhealing wounds.
AB - Disorders of wound healing characterized by impaired or delayed re-epithelialization are a serious medical problem. These conditions affect many tissues, are painful, and are difficult to treat. In this study, using cornea as a model, we demonstrate for the first time the importance of carbohydrate-binding proteins galectins-3 and -7 in re-epithelialization of wounds. In two different models of corneal wound healing, re-epithelialization of wounds was significantly slower in galectin-3-deficient (gal3-/-) mice compared with wild-type (gal3+/+) mice. In contrast, there was no difference in corneal epithelial wound closure rates between galectin-l-deficient and wild-type mice. Quantitation of the bromodeoxyuridine-labeled cells in gal3+/+ and gal3-/- corneas revealed that corneal epithelial cell proliferation rate is not perturbed in gal3-/- corneas. Exogenous galectin-3 accelerated re-epithelialization of wounds in gal3+/+ mice but, surprisingly, not in the gal3-/- mice. Gene expression analysis using cDNA microarrays revealed that healing corneas of gal3-/- mice contain markedly reduced levels of galectin-7 compared with those of gal3+/+ mice. More importantly, unlike galectin-3, galectin-7 accelerated re-epithelialization of wounds in both gal3-/- and gal3+/+ mice. In corresponding experiments, recombinant galectin-1 did not stimulate the corneal epithelial wound closure rate. The extent of acceleration of re-epithelialization of wounds with both galectin-3 and galectin-7 was greater than that observed in most of the published studies using growth factors. These findings have broad implications for developing novel therapeutic strategies for treating nonhealing wounds.
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U2 - 10.1074/jbc.M200981200
DO - 10.1074/jbc.M200981200
M3 - Article
VL - 277
SP - 42299
EP - 42305
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 44
ER -