Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice
- Autores
- Lackey, Atreju I.; Chen, Tina; Zhou, Yin X; Bottasso Arias, Natalia María; Doran, Justine M.; Zacharisen, Sophia M.; Gajda, Angela M.; Jonsson, William O.; Córsico, Betina; Anthony, Tracy G.; Joseph, Laurie B.; Storch, Judith
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Intestinal-fatty acid binding protein (IFABP; FABP2) is a 15-kDa intracellular protein abundantly present in the cytosol of the small intestinal (SI) enterocyte. High-fat (HF) feeding of IFABP-/- mice resulted in reduced weight gain and fat mass relative to wild-type (WT) mice. Here, we examined intestinal properties that may underlie the observed lean phenotype of high fat-fed IFABP-/- mice. No alterations in fecal lipid content were found, suggesting that the IFABP-/- mice are not malabsorbing dietary fat. However, the total excreted fecal mass, normalized to food intake, was increased for the IFABP-/- mice relative to WT mice. Moreover, intestinal transit time was more rapid in the IFABP-/- mice. IFABP-/- mice displayed a shortened average villus length, a thinner muscularis layer, reduced goblet cell density, and reduced Paneth cell abundance. The number of proliferating cells in the crypts of IFABP-/- mice did not differ from that of WT mice, suggesting that the blunt villi phenotype is not due to alterations in proliferation. IFABP-/- mice were observed to have altered expression of genes and proteins related to intestinal structure, while immunohistochemical analyses revealed increased staining for markers of inflammation. Taken together, these studies indicate that the ablation of IFABP, coupled with high-fat feeding, leads to changes in gut motility and morphology, which likely contribute to the relatively leaner phenotype occurring at the whole-body level. Thus, IFABP is likely involved in dietary lipid sensing and signaling, influencing intestinal motility, intestinal structure, and nutrient absorption, thereby impacting systemic energy metabolism.
Instituto de Investigaciones Bioquímicas de La Plata - Materia
-
Bioquímica
Ciencias Exactas
IFABP
Intestine
Lipid
Morphology
Nutrition - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/123452
Ver los metadatos del registro completo
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Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null miceLackey, Atreju I.Chen, TinaZhou, Yin XBottasso Arias, Natalia MaríaDoran, Justine M.Zacharisen, Sophia M.Gajda, Angela M.Jonsson, William O.Córsico, BetinaAnthony, Tracy G.Joseph, Laurie B.Storch, JudithBioquímicaCiencias ExactasIFABPIntestineLipidMorphologyNutritionIntestinal-fatty acid binding protein (IFABP; FABP2) is a 15-kDa intracellular protein abundantly present in the cytosol of the small intestinal (SI) enterocyte. High-fat (HF) feeding of IFABP-/- mice resulted in reduced weight gain and fat mass relative to wild-type (WT) mice. Here, we examined intestinal properties that may underlie the observed lean phenotype of high fat-fed IFABP-/- mice. No alterations in fecal lipid content were found, suggesting that the IFABP-/- mice are not malabsorbing dietary fat. However, the total excreted fecal mass, normalized to food intake, was increased for the IFABP-/- mice relative to WT mice. Moreover, intestinal transit time was more rapid in the IFABP-/- mice. IFABP-/- mice displayed a shortened average villus length, a thinner muscularis layer, reduced goblet cell density, and reduced Paneth cell abundance. The number of proliferating cells in the crypts of IFABP-/- mice did not differ from that of WT mice, suggesting that the blunt villi phenotype is not due to alterations in proliferation. IFABP-/- mice were observed to have altered expression of genes and proteins related to intestinal structure, while immunohistochemical analyses revealed increased staining for markers of inflammation. Taken together, these studies indicate that the ablation of IFABP, coupled with high-fat feeding, leads to changes in gut motility and morphology, which likely contribute to the relatively leaner phenotype occurring at the whole-body level. Thus, IFABP is likely involved in dietary lipid sensing and signaling, influencing intestinal motility, intestinal structure, and nutrient absorption, thereby impacting systemic energy metabolism.Instituto de Investigaciones Bioquímicas de La Plata2020-01-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfG518-G530http://sedici.unlp.edu.ar/handle/10915/123452enginfo:eu-repo/semantics/altIdentifier/issn/1522-1547info:eu-repo/semantics/altIdentifier/issn/0193-1857info:eu-repo/semantics/altIdentifier/pmid/31905021info:eu-repo/semantics/altIdentifier/doi/10.1152/ajpgi.00120.2019info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:29:29Zoai:sedici.unlp.edu.ar:10915/123452Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:29:29.621SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
title |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
spellingShingle |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice Lackey, Atreju I. Bioquímica Ciencias Exactas IFABP Intestine Lipid Morphology Nutrition |
title_short |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
title_full |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
title_fullStr |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
title_full_unstemmed |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
title_sort |
Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice |
dc.creator.none.fl_str_mv |
Lackey, Atreju I. Chen, Tina Zhou, Yin X Bottasso Arias, Natalia María Doran, Justine M. Zacharisen, Sophia M. Gajda, Angela M. Jonsson, William O. Córsico, Betina Anthony, Tracy G. Joseph, Laurie B. Storch, Judith |
author |
Lackey, Atreju I. |
author_facet |
Lackey, Atreju I. Chen, Tina Zhou, Yin X Bottasso Arias, Natalia María Doran, Justine M. Zacharisen, Sophia M. Gajda, Angela M. Jonsson, William O. Córsico, Betina Anthony, Tracy G. Joseph, Laurie B. Storch, Judith |
author_role |
author |
author2 |
Chen, Tina Zhou, Yin X Bottasso Arias, Natalia María Doran, Justine M. Zacharisen, Sophia M. Gajda, Angela M. Jonsson, William O. Córsico, Betina Anthony, Tracy G. Joseph, Laurie B. Storch, Judith |
author2_role |
author author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Bioquímica Ciencias Exactas IFABP Intestine Lipid Morphology Nutrition |
topic |
Bioquímica Ciencias Exactas IFABP Intestine Lipid Morphology Nutrition |
dc.description.none.fl_txt_mv |
Intestinal-fatty acid binding protein (IFABP; FABP2) is a 15-kDa intracellular protein abundantly present in the cytosol of the small intestinal (SI) enterocyte. High-fat (HF) feeding of IFABP-/- mice resulted in reduced weight gain and fat mass relative to wild-type (WT) mice. Here, we examined intestinal properties that may underlie the observed lean phenotype of high fat-fed IFABP-/- mice. No alterations in fecal lipid content were found, suggesting that the IFABP-/- mice are not malabsorbing dietary fat. However, the total excreted fecal mass, normalized to food intake, was increased for the IFABP-/- mice relative to WT mice. Moreover, intestinal transit time was more rapid in the IFABP-/- mice. IFABP-/- mice displayed a shortened average villus length, a thinner muscularis layer, reduced goblet cell density, and reduced Paneth cell abundance. The number of proliferating cells in the crypts of IFABP-/- mice did not differ from that of WT mice, suggesting that the blunt villi phenotype is not due to alterations in proliferation. IFABP-/- mice were observed to have altered expression of genes and proteins related to intestinal structure, while immunohistochemical analyses revealed increased staining for markers of inflammation. Taken together, these studies indicate that the ablation of IFABP, coupled with high-fat feeding, leads to changes in gut motility and morphology, which likely contribute to the relatively leaner phenotype occurring at the whole-body level. Thus, IFABP is likely involved in dietary lipid sensing and signaling, influencing intestinal motility, intestinal structure, and nutrient absorption, thereby impacting systemic energy metabolism. Instituto de Investigaciones Bioquímicas de La Plata |
description |
Intestinal-fatty acid binding protein (IFABP; FABP2) is a 15-kDa intracellular protein abundantly present in the cytosol of the small intestinal (SI) enterocyte. High-fat (HF) feeding of IFABP-/- mice resulted in reduced weight gain and fat mass relative to wild-type (WT) mice. Here, we examined intestinal properties that may underlie the observed lean phenotype of high fat-fed IFABP-/- mice. No alterations in fecal lipid content were found, suggesting that the IFABP-/- mice are not malabsorbing dietary fat. However, the total excreted fecal mass, normalized to food intake, was increased for the IFABP-/- mice relative to WT mice. Moreover, intestinal transit time was more rapid in the IFABP-/- mice. IFABP-/- mice displayed a shortened average villus length, a thinner muscularis layer, reduced goblet cell density, and reduced Paneth cell abundance. The number of proliferating cells in the crypts of IFABP-/- mice did not differ from that of WT mice, suggesting that the blunt villi phenotype is not due to alterations in proliferation. IFABP-/- mice were observed to have altered expression of genes and proteins related to intestinal structure, while immunohistochemical analyses revealed increased staining for markers of inflammation. Taken together, these studies indicate that the ablation of IFABP, coupled with high-fat feeding, leads to changes in gut motility and morphology, which likely contribute to the relatively leaner phenotype occurring at the whole-body level. Thus, IFABP is likely involved in dietary lipid sensing and signaling, influencing intestinal motility, intestinal structure, and nutrient absorption, thereby impacting systemic energy metabolism. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-01-06 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/123452 |
url |
http://sedici.unlp.edu.ar/handle/10915/123452 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/1522-1547 info:eu-repo/semantics/altIdentifier/issn/0193-1857 info:eu-repo/semantics/altIdentifier/pmid/31905021 info:eu-repo/semantics/altIdentifier/doi/10.1152/ajpgi.00120.2019 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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application/pdf G518-G530 |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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