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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/123452

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network_name_str SEDICI (UNLP)
spelling 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)
dc.format.none.fl_str_mv application/pdf
G518-G530
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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