scholarly journals PROTEIN-LOSING ENTEROPATHY AFTER INFECTIOUS ENTEROCOLITIS IN CHILD – A CASE REPORT AND A REVIEW OF THE LITERATURE

2017 ◽  
Vol 20 (1) ◽  
pp. 26-30
Author(s):  
Lorena Elena Melit ◽  
◽  
Cristina Oana Marginean ◽  
Andreea Dinca ◽  
Raluca Damian ◽  
...  
Keyword(s):  
Severe Case ◽  
Female Child ◽  
Fecal Calprotectin ◽  
Human Albumin ◽  
Protein Loss ◽  
Small Female ◽  
Protein Losing Enteropathy ◽  
E Coli ◽  
Alpha 1 Antitrypsin ◽  
Infectious Enterocolitis

Protein-losing enteropathy (PLE) represents an abnormal protein loss at the level of the digestive tract mucosa, being in most of the cases secondary to other gastrointestinal or extraintestinal pathologies. Nevertheless, there also are primary causes, genetic ones associated with PLE. We present the case of a small female child, 1 year and 1 month-old, with a history of infectious enterocolitis determined by Escherichia coli enteropathogenic, who presented palpebral edemas, especially in the morning for approximately 1 week. The laboratory tests revealed hypoalbuminemia, type A and G hypogammaglobulinemia, leukocytosis with eosinophilia, and anemia. The test for the detection of occult hemorrhages from feces was positive, likewise the fecal calprotectin and level of alpha-1 antitrypsin. We identified also allergy to cow’s milk protein, which we interpreted as being secondary to the intestinal pathology. Thus, we established the diagnosis of protein losing enteropathy after an episode of acute enterocolitis caused by E. coli enteropathogenic, and we administered substitutive treatment with human albumin and steroids, with favorable evolution. The particularity of the case consists in diagnosing a severe case of protein-losing enteropathy in a small child, with palpebral edema, predominantly during the morning, and decreased levels of serum albumin, after an episode of acute enterocolitis caused by E. coli enteropathogenic, which remitted without etiologic treatment.

scholarly journals Gut wall integrity in exclusively breastfed vs. formula-fed infants

2016 ◽  
Vol 56 (4) ◽  
pp. 199
Author(s):  
Nur Hayati ◽  
Muzal Kadim ◽  
Irawan Mangunatmadja ◽  
Soepardi Soedibyo ◽  
Evita Bermansyah Ifran ◽  
...  
Keyword(s):  
Breast Milk ◽  
Immunoglobulin A ◽  
Fecal Calprotectin ◽  
Protein Loss ◽  
Bioactive Substances ◽  
Mucosal Integrity ◽  
Healthy Infants ◽  
Feeding Type ◽  
Calprotectin Level ◽  
Alpha 1 Antitrypsin

Background Breast milk has bioactive substances that modulate gastrointestinal maturation and maintain mucosal integrity of the gut in infants. Markers that are both non-invasive and reliable, such as fecal alpha-1 antitrypsin (AAT), calprotectin, and secretory immunoglobulin A (sIgA) have been used to assess gut integrity in adults. Higher AAT levels may imply greater enteric protein loss due to increase intestinal permeability of immaturity gut.Objective To assess and compare gut integrity of exclusively breastfed (BF) and exclusively formula fed (FF) infants aged 4-6 months.Methods Subjects were 80 healthy infants (BF=40; FF=40), aged 4-6 months who visited the Pediatric Polyclinic at St. Carolus Hospital, and lived in Pasar Minggu or Cempaka Putih Districts, Jakarta. The fecal AAT was analyzed by an ELISA method. Mann-Whitney and unpaired T-test were used to analyze possible correlations between feeding type and gut integrity.Results The BF group had significantly higher mean fecal AAT than the FF group (P=0.02). Median sIgA levels were not significantly different between groups (P=0.104). The FF group had a higher mean fecal calprotectin level but this difference was also not significant (P=0.443). There was a significant correlation between breastfeeding and mean fecal AAT level (P=0.02), but no significant correlation with calprotectin (P=0.65) or sIgA (P=0.26).Conclusion The breastfed group shows better mucosal integrity compared to the formula fed group. Higher mean fecal AAT level in the BF group is related to the AAT content of breast milk. Therefore AAT content of BF group is actually lower than formula fed group which shows greater mucosal integrity in BF group.

scholarly journals Fecal alpha-1 antitrypsin concentration in protein-losing enteropathies caused by Rotavirus and enteropathogenic bacteria infection

2009 ◽  
Vol 49 (6) ◽  
pp. 315
Author(s):  
D. Aulia ◽  
I. S. Timan ◽  
A. Firmansyah
Keyword(s):  
Acute Diarrhea ◽  
Intestinal Inflammation ◽  
Protein Loss ◽  
Chi Square ◽  
Rotavirus Infection ◽  
E Coli ◽  
Enteropathogenic Bacteria ◽  
The Mean ◽  
Alpha 1 Antitrypsin ◽  
The Relationship

Background An increase in protein loss through the intestinallumen is commonly found in children with intestinal inflammation. Measurement of fecal alpha-1 antitrypsin (FAA T) concentration has been used to detect the loss of protein through the digestive system. FAAT concentration increases in diarrhea patients due to Rotavirus, Adenovirus, Shigella, Enterotoxigenic E. coli (ETEC), and Salmonella infection.Objective To determine the relationship between types ofpathogen, acute diarrhea, and alpha-1 antitrypsin concentrationin children with acute diarrhea caused by Rotavirus andenteropathogenic infection.Methods Descriptive statistics and proportion difference betweenthe two non-related groups were used to assess the proportion ofprotein-losing enteropathy (PLE) in children with acute diarrheaand was analyzed using chi square test.Results In this study, PLE group comprised 25% (24/95) subjectswithout unknown cause of diarrhea, 50% (4 7 /95) had one typeof pathogen, and in 23% (22/95) subjects had 2 or more types of pathogens. The most common pathogen found in PLE group was Rotavirus, found in67 (53%) subjects and E. coli in 41 (33%) subjects. In non-PLE group, we also found similar pathogen pattern. The mean alpha-1 antitrypsin (AAT) concentration in acute diarrhea group due to Rotavirus infection was significantly higher (P= 0.003) compared to acute diarrhea groups caused by non-Rotavirus infection. The mean AAT concentration in acute diarrhea group due to E. coli infection did not differ significantly (P= 0.735) compared to acute diarrhea group caused by non-E. coli infection.Conclusion Rotavirus was a more significant cause of PLEcompared to E.coli.

New insights in gut-liver axis in wild-type murine imiquimod-induced lupus

Lupus ◽  
2021 ◽  
Vol 30 (6) ◽  
pp. 926-936
Author(s):  
Georges Maalouly ◽  
Joelle Hajal ◽  
Charbel Noujeim ◽  
Michel Choueiry ◽  
Hussein Nassereddine ◽  
...  
Keyword(s):  
Tight Junction ◽  
Fecal Calprotectin ◽  
Liver Inflammation ◽  
Tight Junction Proteins ◽  
Wild Type ◽  
Imiquimod Cream ◽  
E Coli ◽  
Intestinal Pathology ◽  
Nfκb Pathway ◽  
Junction Proteins

Background Intestinal and hepatic manifestations of lupus seem to be underestimated in comparison to other major organ lesions. Although recent data point to gut-liver axis involvement in lupus, gut permeability dysfunction and liver inflammation need to be more investigated. Objective This study aims to assess fecal calprotectin, intestinal tight junction proteins and liver inflammation pathway in wild-type murine imiquimod- induced lupus. Methods C57BL/6 mice were topically treated on their right ears with 1.25 mg of 5% imiquimod cream, three times per week for six weeks. Fecal calprotectin was collected at day 0, 22 and 45. Renal, liver and intestinal pathology, as well as inflammatory markers, intestinal tight junction proteins, and E. coli protein in liver were assessed at sacrifice. Results At six weeks, lupus nephritis was confirmed on histopathology and NGAL and KIM-1 expression. Calprotectin rise started at day 22 and persists at day 45. Protein expression of Claudine, ZO-1 and occludin was significantly decreased. E. coli protein was significantly increased in liver with necro-inflammation and increased TLR4, TLR7, and pNFκB/NFκB liver expression. Conclusion This study is the first to demonstrate early fecal calprotectin increase and liver activation of TLR4- NFκB pathway in wild-type murine imiquimod-induced lupus.

Unusual presentation of Crohn’s disease

2021 ◽  
Vol 14 (6) ◽  
pp. e242703
Author(s):  
Kate Edwards ◽  
Karen Yearsley
Keyword(s):  
Crohn’S Disease ◽  
Small Bowel ◽  
Crohn's Disease ◽  
Wedge Resection ◽  
Rare Condition ◽  
Unusual Presentation ◽  
Protein Losing Enteropathy ◽  
Inflammatory Bowel ◽  
Alpha 1 Antitrypsin ◽  
Underlying Pathophysiology

A previously well 37-year-old woman attended the emergency assessment unit with symptoms of lethargy, breathlessness and peripheral oedema, whereby initial basic investigations revealed an iron deficiency anaemia and serum hypoalbuminaemia. The patient subsequently had multiple admissions to secondary care over a 2-year period due to worsening peripheral and central oedema. Investigations ruled out non-gastrointestinal causes of serum hypoalbuminaemia, such as renal, cardiac and hepatic failures. Gastrointestinal investigations later revealed raised faecal alpha-1 antitrypsin and small bowel ulceration on capsule endoscopy, with a histological diagnosis of Crohn’s disease made after a small bowel wedge resection. This case describes the unusual presentation of Crohn’s disease displaying symptoms primarily of protein-losing enteropathy, an uncommon and under-recognised consequence of inflammatory bowel disease. A review of current literature and the underlying pathophysiology for this rare condition are discussed, particularly in relation to Crohn’s disease.

Clostridium Difficile Infection and Biliary Obstruction

2021 ◽  
Vol 8 (1) ◽  
pp. 01-06
Author(s):  
Marilena Stoian
Keyword(s):  
Inflammatory Bowel Disease ◽  
Clostridium Difficile ◽  
Clostridium Difficile Infection ◽  
Crohn Disease ◽  
Bowel Disease ◽  
Biliary Obstruction ◽  
Hepatobiliary Disease ◽  
Protein Loss ◽  
Protein Losing Enteropathy ◽  
Inflammatory Bowel

We present a case of a 38-year -old man was admitted to the hospital with biliary obstruction and Clostridium Difficile infection. He presented with moderate increases in the aminotransferase and bilirubin levels suggesting the diagnosis of an autoimmune hepatobiliary disease; intestinal protein loss needs to evaluate an associated inflammatory bowel disease. The clinical diagnosis of autoimmune hepatobiliary disease associated with inflammatory bowel disease is based on the patients symptoms and the presence of a protein-losing enteropathy which are more suggestive of Crohn disease, while moderate increases in the aminotransferase levels in proportion to the increase in the bilirubin level suggesting the diagnosis of primary sclerosing cholangitis. The pathological and positive diagnosis needs an endoscopic retrograde cholangiopancreatography and a biopsy of gastric and duodenum mucosae who showed severe inflammation findings that are diagnostic of Crohn disease.

Evaluation of Human Fecal Calprotectin Detection Kits and Their Potential use as Non-Invasive Intestinal Biomarker of Infectious Enterocolitis in Pigs

2021 ◽  
Author(s):  
Jéssica Barbosa ◽  
Lucas Rodrigues ◽  
Daniel Columbus ◽  
Juan Aguirre ◽  
John Harding ◽  
...  
Keyword(s):  
Intestinal Inflammation ◽  
Point Of Care ◽  
Sandwich Elisa ◽  
Fecal Calprotectin ◽  
Field Application ◽  
Dipstick Test ◽  
Infectious Colitis ◽  
Fecal Samples ◽  
Non Invasive ◽  
Infectious Enterocolitis

Abstract Background: Fecal calprotectin is largely applied as a non-invasive intestinal inflammation biomarker in human medicine. Previous studies in pigs investigated the levels of fecal calprotectin in healthy animals only. Thus, there is a knowledge gap regarding its application during infectious diarrhea. This study investigated the usefulness of fecal calprotectin as a biomarker of intestinal inflammation in Brachyspira hyodysenteriae and Salmonella Typhimurium infected pigs. Results: Fecal samples from pigs with colitis (n=18) were collected from animals experimentally inoculated with B. hyodysenteriae G44 or from sham-inoculated controls. Fecal samples from pigs with enteritis (n=14) were collected from animals inoculated with Salmonella enterica serovar Typhimurium or from sham-inoculated controls. For both groups, fecal samples were scored as: 0 = normal; 1 = soft, wet cement; 2 = watery feces; 3 = mucoid diarrhea; and 4 = bloody diarrhea. Fecal calprotectin levels were assayed using a sandwich ELISA, a turbidimetric immunoassay and a point-of-care dipstick test. Fecal calprotectin levels were greater in colitis samples scoring 4 versus ≤ 4 using ELISA, and in feces scoring 3 and 4 versus ≤ 1 using immunoturbidimetry (P < 0.05). No differences were found in calprotectin concentration among fecal scores for enteritis samples, regardless of the assay used. All samples were found below detection limits using the dipstick method.Conclusions: Fecal calprotectin is a potential non-invasive biomarker of infectious colitis, but it is not suitable for detection of enteritis. While practical, the use of commercially available human presents sensitivity limitations. Further studies are needed to validate the field application of calprotectin as a marker.

Persistence of Protein Loss in Acute Diarrhoea: A Follow-up Study by Faecal Alpha-1-Antitrypsin Measurement

1991 ◽  
Vol 80 (10) ◽  
pp. 961-963 ◽  
Author(s):  
G. Zuin ◽  
M. Fontana ◽  
S. Nicoli ◽  
L. Scapellato ◽  
G. Tamburini ◽  
...  
Keyword(s):  
Acute Diarrhoea ◽  
Protein Loss ◽  
Follow Up Study ◽  
Alpha 1 Antitrypsin

scholarly journals A comparison of the unfolding and dissociation of the large ribosome subunits from Rhodopseudomonas·spheroides N.C.I.B. 8253 and Escherichia coli M.R.E. 600

1973 ◽  
Vol 133 (4) ◽  
pp. 739-747 ◽  
Author(s):  
A. Robinson ◽  
J. Sykes
Keyword(s):  
Escherichia Coli ◽  
Protein Interactions ◽  
Ribosomal Proteins ◽  
Ribosomal Subunit ◽  
23S Rrna ◽  
Core Particle ◽  
Protein Loss ◽  
E Coli ◽  
Rrna Species ◽  
Rhodopseudomonas Spheroides

1. The behaviour of the large ribosomal subunit from Rhodopseudomonas spheroides (45S) has been compared with the 50S ribosome from Escherichia coli M.R.E. 600 (and E. coli M.R.E. 162) during unfolding by removal of Mg2+ and detachment of ribosomal proteins by high univalent cation concentrations. The extent to which these processes are reversible with these ribosomes has also been examined. 2. The R. spheroides 45S ribosome unfolds relatively slowly but then gives rise directly to two ribonucleoprotein particles (16.6S and 13.7S); the former contains the intact primary structure of the 16.25S rRNA species and the latter the 15.00S rRNA species of the original ribosome. No detectable protein loss occurs during unfolding. The E. coli ribosome unfolds via a series of discrete intermediates to a single, unfolded ribonucleoprotein unit (19.1S) containing the 23S rRNA and all the protein of the original ribosome. 3. The two unfolded R. spheroides ribonucleoproteins did not recombine when the original conditions were restored but each simply assumed a more compact configuration. Similar treatments reversed the unfolding of the E. coli 50S ribosomes; replacement of Mg2+ caused the refolding of the initial products of unfolding and in the presence of Ni2+ the completely unfolded species (19.1S) again sedimented at the same rate as the original ribosomes (44S). 4. Ribosomal proteins (25%) were dissociated from R. spheroides 45S ribosomes by dialysis against a solution with a Na+/Mg2+ ratio of 250:1. During this process two core particles were formed (21.2S and 14.2S) and the primary structures of the two original rRNA species were conserved. This dissociation was not reversed. With E. coli 50S approximately 15% of the original ribosomal protein was dissociated, a single 37.6S core particle was formed, the 23S rRNA remained intact and the ribosomal proteins would reassociate with the core particle to give a 50S ribosome. 5. The ribonuclease activities in R. spheroides 45S and E. coli M.R.E. 600 and E. coli M.R.E. 162 50S ribosomes are compared. 6. The observations concerning unfolding and dissociation are consistent with previous reports showing the unusual rRNA complement of the mature R. spheroides 45S ribosome and show the dependence of these events upon the rRNA and the importance of protein–protein interactions in the structure of the R. spheroides ribosome.

Establishing the role of PLVAP in protein-losing enteropathy: a homozygous missense variant leads to an attenuated phenotype

2018 ◽  
Vol 55 (11) ◽  
pp. 779-784 ◽  
Author(s):  
Alina Kurolap ◽  
Orly Eshach-Adiv ◽  
Claudia Gonzaga-Jauregui ◽  
Katya Dolnikov ◽  
Adi Mory ◽  
...  
Keyword(s):  
Barrier Function ◽  
Protein Function ◽  
Transmembrane Domain ◽  
Autosomal Recessive Inheritance ◽  
Missense Variant ◽  
Protein Loss ◽  
Protein Losing Enteropathy ◽  
Family Based ◽  
And Function

BackgroundIntestinal integrity is essential for proper nutrient absorption and tissue homeostasis, with damage leading to enteric protein loss, that is, protein-losing enteropathy (PLE). Recently, homozygous nonsense variants in the plasmalemma vesicle-associated protein gene (PLVAP) were reported in two patients with severe congenital PLE. PLVAP is the building block of endothelial cell (EC) fenestral diaphragms; its importance in barrier function is supported by mouse models of Plvap deficiency.ObjectiveTo genetically diagnose two first-degree cousins once removed, who presented with PLE at ages 22 and 2.5 years.MethodsFamily-based whole exome sequencing was performed based on an autosomal recessive inheritance model. In silico analyses were used to predict variant impact on protein structure and function.ResultsWe identified a rare homozygous variant (NM_031310.2:c.101T>C;p.Leu34Pro) in PLVAP, which co-segregated with the disease. Leu34 is predicted to be located in a highly conserved, hydrophobic, α-helical region within the protein’s transmembrane domain, suggesting Leu34Pro is likely to disrupt protein function and/or structure. Electron microscopy and PLVAP immunohistochemistry demonstrated apparently normal diaphragm morphology, predicted to be functionally affected.ConclusionsBiallelic missense variants in PLVAP can cause an attenuated form of the PLE and hypertriglyceridaemia syndrome. Our findings support the role of PLVAP in the pathophysiology of PLE, expand the phenotypic and mutation spectrums and underscore PLVAP’s importance in EC barrier function in the gut.

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