title: Contribution of villous atrophy to reduced intestinal maltase in infants with malnutrition.
abstract: BACKGROUND
  It has been known for many years that small intestinal maltase activities are reduced in malnourished infants and in other patients with villous atrophy. The recent availability of human maltase-glucoamylase cDNA provides the opportunity to test the hypothesis that villous atrophy accounts for the reduced maltase enzyme activity in malnourished infants.
  
  
  METHODS
  Mucosal biopsy specimens obtained for clinical evaluation of malnourished infants with poor responses to refeeding were examined by quantitative methods for enzyme activity and mRNA levels.
  
  
  RESULTS
  Maltase activity and maltase-glucoamylase mRNA were reduced (approximately 45% of normal). When maltase-glucoamylase message was normalized to villin message, a structural protein expressed only in enterocytes, a preservation of maltase messages in surviving enterocytes was documented. The luminal glucose transporter-villin message was also preserved.
  
  
  CONCLUSIONS
  The loss of maltase-glucoamylase message paralleled the reduction in villin message and degree of villous atrophy. The reduced maltase-glucoamylase message also paralleled sucrase-isomaltase message, previously found to be decreased in proportion to villous atrophy of malnourished infants. The data directly demonstrate, for the first time, that the terminal steps of starch 1-4 starch digestion and sucrase-isomaltase 1-6 starch digestion are decreased in malnourished infants, secondary to villous atrophy. These data in prior and present reports suggest that mechanisms underlying the chronic villous atrophy of malnutrition should be a priority for investigations in malnourished infants with slower than expected weight gain during refeeding.
authors.affiliation: U.S. Department of Agriculture/Agriculture Research Service, Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine and Texas Children's Hospital, Houston 77030-2600, USA.
authors.forename: B L
authors.initials: BL
authors.lastname: Nichols
authors.forename: V N
authors.initials: VN
authors.lastname: Nichols
authors.forename: M
authors.initials: M
authors.lastname: Putman
authors.forename: S E
authors.initials: SE
authors.lastname: Avery
authors.forename: J K
authors.initials: JK
authors.lastname: Fraley
authors.forename: A
authors.initials: A
authors.lastname: Quaroni
authors.forename: M
authors.initials: M
authors.lastname: Shiner
authors.forename: E E
authors.initials: EE
authors.lastname: Sterchi
authors.forename: F R
authors.initials: FR
authors.lastname: Carrazza
mesh_terms: D000199:Actins / Q000235:genetics; D001284:Atrophy; D001706:Biopsy; D002352:Carrier Proteins / Q000235:genetics; D002675:Child, Preschool; D005260:Female; D006801:Humans; D007223:Infant; D007413:Intestinal Mucosa / Q000201:enzymology / Q000473:pathology; D007422:Intestines / Q000201:enzymology* / Q000473:pathology*; D008297:Male; D008562:Membrane Glycoproteins / Q000235:genetics; D008840:Microfilament Proteins / Q000235:genetics; D009004:Monosaccharide Transport Proteins / Q000235:genetics; D009748:Nutrition Disorders / Q000201:enzymology* / Q000473:pathology*; D009752:Nutritional Status; D012333:RNA, Messenger / Q000378:metabolism; D051269:Sodium-Glucose Transporter 1; D000520:alpha-Glucosidases / Q000235:genetics / Q000378:metabolism*
chemical_list: D000199:Actins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D008840:Microfilament Proteins; D009004:Monosaccharide Transport Proteins; D012333:RNA, Messenger; D051269:Sodium-Glucose Transporter 1; C026615:villin; D000520:alpha-Glucosidases