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2. Intestinal alkaline phosphatase prevents metabolic syndrome in mice

Author

Kaliannan, Kanakaraju, Hamarneh, Sulaiman R., Economopoulos, Konstantinos P., Alam, Sayeda Nasrin, Moaven, Omeed, Patel, Palak, Malo, Nondita S., Ray, Madhury, Abtahi, Seyed M., Muhammad, Nur, Raychowdhury, Atri, Teshager, Abeba, Mohamed, Mussa M. Rafat, Moss, Angela K., Ahmed, Rizwan, Hakimian, Shahrad, Narisawa, Sonoko, Millán, José Luis, Hohmann, Elizabeth, Warren, H. Shaw, Bhan, Atul K., Malo, Madhu S., and Hodin, Richard A.

Published
2013

3. Intestinal alkaline phosphatase deficiency increases the risk of diabetes

Author

Malo, Jagannath, Alam, Md Jahangir, Islam, Salequl, Mottalib, Md Abdul, Rocki, Md Mehedi Hasan, Barmon, Ginok, Tinni, Shamema Akter, Barman, Swapan K, Sarker, Tapas, Khan, Md Nayeemul Islam, Kaliannan, Kanakaraju, Hasanat, Muhammad Abul, Rahman, Salimur, Pathan, Md Faruque, Khan, A K Azad, and Malo, Madhu S

Subjects
Adult, Incidence, Endocrinology, Diabetes and Metabolism, Fasting, Middle Aged, Alkaline Phosphatase, RC648-665, Diseases of the endocrine glands. Clinical endocrinology, type 2, Diabetes Mellitus, Type 2, diabetes mellitus, Humans, Epidemiology/Health services research, Obesity
Abstract

IntroductionOur previous case–control study demonstrated that a high level of intestinal alkaline phosphatase (IAP), an endotoxin-detoxifying anti-inflammatory enzyme secreted by villus-associated enterocytes and excreted with stool, plays a protective role against type 2 diabetes mellitus (T2DM) irrespective of obesity. In the current study, we investigated the long-term effect of IAP deficiency (IAPD) on the pathogenesis of T2DM.Research design and methodsA healthy cohort of participants without diabetes (30–60 years old), comprising 188 without IAPD (IAP level: ≥65 U/g stool) and 386 with IAPD (IAP level: ResultsT2DM incidence rates were 8.0%, 11.7%, 25.6%, and 33.3% in participants with ‘persistent no IAPD’ (IAP level: always ≥65 U/g stool), ‘remittent IAPD’ (IAP level: increased from 2 p=0.0541). Sensitivity analyses of persistent IAP levels revealed that, compared with participants of the highest persistent IAP pentile (always >115 U/g stool), the rate of increase of fasting glycemia was double and the risk of developing T2DM was 1280% higher (RR: 13.80 (95% CI 1.87 to 101.3), p=0.0099) in participants of the lowest persistent IAP pentile (always ConclusionsIAPD increases the risk of developing T2DM, and regular STAP tests would predict individual vulnerability to T2DM. Oral IAP supplementation might prevent T2DM.

Published
2022

6. Identification of specific targets for the gut mucosal defense factor intestinal alkaline phosphatase

Author

Chen, Kathryn T., Malo, Madhu S., Moss, Angela K., Zeller, Skye, Johnson, Paul, Ebrahimi, Farzad, Mostafa, Golam, Alam, Sayeda N., Ramasamy, Sundaram, Warren, H. Shaw, Hohmann, Elizabeth L., and Hodin, Richard A.

Subjects
Gastrointestinal mucosa -- Properties, Alkaline phosphatase -- Health aspects, Lipopolysaccharides -- Health aspects, Cell receptors -- Properties, Digestion -- Research, Biological sciences
Abstract

Intestinal alkaline phosphatase (IAP) is a small intestinal brush border enzyme that has been shown to function as a gut mucosal defense factor, but its precise mechanism of action remains unclear. We investigated the effects of IAP on specific bacteria and bacterial components to determine its molecular targets. Purulent fluid from a cecal ligation and puncture model, specific live and heat-killed bacteria (Escherichia coil, Salmonella typhimurium, and Listeria monocytogenes), and a variety of proinflammatory ligands (LPS, CpG DNA, Pam-3-Cys, flagellin, and TNF) were incubated with or without calf IAP (cIAP). Phosphate release was determined by using a malachite green assay. The various fluids were applied to target cells (THP-1, parent HT-29, and IAP-expressing HT-29 cells) and IL-8 secretion measured by ELISA. cIAP inhibited IL-8 induction by purulent fluid in THP-1 cells by >35% (P < 0.005). HT29-IAP cells had a reduced IL-8 response specifically to gram-negative bacteria; >90% reduction compared with parent cells (P < 0.005). cIAP had no effect on live bacteria but attenuated IL-8 induction by heat-killed bacteria by >40% (P < 0.005). cIAP exposure to LPS and CpG DNA caused phosphate release and reduced IL-8 in cell culture by >50% (P < 0.005). Flagellin exposure to cIAP also resulted in reduced IL-8 secretion by >40% (P < 0.005). In contrast, cIAP had no effect on TNF or Pam-3-Cys. The mechanism of IAP action appears to be through dephosphorylation of specific bacterial components, including LPS, CpG DNA, and flagellin, and not on live bacteria themselves. IAP likely targets these bacterially derived molecules in its role as a gut mucosal defense factor. lipopolysaccharide; Toll-like receptors doi: 10.1152/ajpgi.00364.2009.

Published
2010

7. Phosphate Groups in the Lipid A Moiety Determine the Effects of LPS on Hepatic Stellate Cells: A Role for LPS-Dephosphorylating Activity in Liver Fibrosis

Author

Schippers, Marlies, primary, Post, Eduard, additional, Eichhorn, Ilse, additional, Langeland, Jitske, additional, Beljaars, Leonie, additional, Malo, Madhu S., additional, Hodin, Richard A., additional, Millán, José Luis, additional, Popov, Yury, additional, Schuppan, Detlef, additional, and Poelstra, Klaas, additional

Published
2020
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8. Intestinal alkaline phosphatase gene expression is activated by ZBP-89

Author

Malo, Madhu S., Mozumder, Moushumi, Zhang, Xiao Bo, Biswas, Shaluk, Chen, Alexander, Bai, Long-Chuan, Merchant, Juanita L., and Hodin, Richard A.

Subjects
Carcinogenesis -- Research, Carcinogenesis -- Analysis, Eukaryotes -- Research, Colorectal diseases -- Research, Colorectal diseases -- Analysis, Gastrointestinal diseases -- Research, Gastrointestinal diseases -- Analysis, Biological sciences
Abstract

Intestinal alkaline phosphatase (IAP) is an enterocyte differentiation marker that functions to limit fat absorption. Zinc finger binding protein-89 (ZBP-89) is a Kruppel-type transcription factor that appears to promote a differentiated phenotype in the intestinal epithelium. The purpose of this study was to investigate the regulation of IAP gene expression by ZBP-89. RT-PCR, quantitative real-time RT-PCR, Western blot analyses, and reporter assays were used to determine the regulation of IAP by ZBP-89 in HT-29 and Caco-2 colon cancer cells. ZBP-89 knockdown was achieved by specific short interfering (si)RNA. EMSA and chromatin immunoprecipitation (CHIP) were performed to examine the binding of ZBP-89 to the IAP promoter. The results of RT-PCR, quantitative real-time PCR, and Western blot analyses showed that ZBP-89 was expressed at low levels in Caco-2 and HT-29 cells, whereas IAP was minimally expressed and absent in these cells, respectively. Transfection with ZBP-89 expression plamid increased IAP mRNA and protein levels in both cell lines, whereas knockdown of endogenous ZBP-89 by siRNA reduced basal levels of IAP gene expression in Caco-2 cells. IAP-luciferase reporter assays, EMSA, and ChIP established that ZBP-89 activated the IAP gene through a response element (ZBP-89 response element: 5'-CCTCCTCCC-3') located between -1018 and -1010 bp upstream of the AUG start codon. We conclude that ZBP-89 is a direct transcriptional activator of the enterocyte differentiation marker IAP. These findings are consistent with the role that this transcription factor is thought to play as a tumor suppressor and suggests its possible function in the physiology of fat absorption. carcinogenesis; development; enterocyte differentiation; eukaryotic promoter; transient transfection

Published
2006

9. Differential regulation of intestinal alkaline phosphatase gene expression by Cdx1 and Cdx2

Author

Alkhoury, Fuad, Malo, Madhu S., Mozumder, Moushumi, Mostafa, Golam, and Hodin, Richard A.

Subjects
Genetic transcription -- Research, Intestines -- Research, Epithelial cells -- Research, Biological sciences
Abstract

We have examined the role that the caudal-related homeobox transcription factors Cdx1 and Cdx2 play in activating the enterocyte differentiation marker gene intestinal alkaline phosphatase (IAP). Human colon cancer Caco-2 cells were transiently transfected with Cdx1 and/or Cdx2, and semiquantitative RT-PCR was used to study the effects on IAP mRNA expression. Transfections with a variety of IAP-luciferase reporter constructs were used to identify a Cdx response element located within the human IAP gene promoter. Protein-DNA interactions were examined by EMSA. Results showed that Cdx1 markedly induced IAP mRNA expression, whereas Cdx2 did not, and, in fact, inhibited the Cdx1 effects. Functional analysis revealed that Cdx1 transactivates (fourfold, P < 0.05) the IAP promoter through a novel Cdx response element (GTTTAGA) located between -2369 and -2375 upstream of the translational start site. EMSA showed that both Cdx1 and Cdx2 could bind to the cis element, but in cotransfection experiments, Cdx2 inhibited the Cdx1 effects by ~50%. Thus we have identified a previously unrecognized interaction between two important gut transcription factors, Cdx1 and Cdx2, in the context of IAP gene regulation. Cdx1 activates the IAP gene via a novel cis element, whereas Cdx2 inhibits the Cdx1 effects. cell cycle; enterocyte differentiation; gene regulation; gut development; homeostasis; intestinal alkaline phosphatase; tumorigenesis

Published
2005

12. Enterocyte differentiation marker intestinal alkaline phosphatase is a target gene of the gut-enriched Kruppel-like factor

Author

Hinnebusch, Brian F., Siddique, Aleem, Henderson, J. Welles, Malo, Madhu S., Zhang, Wenying, Athaide, Christopher P., Abedrapo, Mario A., Chen, Xinming, Yang, Vincent W., and Hodin, Richard A.

Subjects
Intestines -- Research, Biological sciences
Abstract

We have examined the role that the transcription factor gut-enriched Kruppel-like factor (KLF4 or GKLF) plays in activating the enterocyte differentiation marker gene intestinal alkaline phosphatase (IAP). A yeast one-hybrid screen was used to identify proteins interacting with a previously identified cis-element (IF-III) located within the human IAP gene promoter. DNA-protein interactions were determined by using EMSA. Northern blot analysis was used to study RNA expression in human colon cancer RKO cells engineered to overexpress KLF4. Transient transfections with IAP-luciferase reporter constructs were used to characterize the mechanisms by which KLF4 activates IAP transcription. The yeast one-hybrid screen and EMSA identified KLF4 as binding to IF-III. RKO cells induced to overexpress KLF4 demonstrated a corresponding dose-dependent increase in IAP expression, and EMSA with nuclear extract from these cells confirmed that KLF4 binds to the IF-III element. Transient transfections revealed that KLF4 transactivated the IAP gene largely via a critical segment in the IAP promoter that includes the IF-IIII cis-element. Mutant KLF4 constructs failed to fully activate IAP. We have identified the enterocyte differentiation marker IAP as a KLF4 target gene. IAP transactivation by KLF4 is likely mediated through a critical region located within the proximal IAP promoter region. intestine; transcription factor; gene regulation

Published
2004

13. Intestinal alkaline phosphatase targets the gut barrier to prevent aging

Author

Kühn, Florian, primary, Adiliaghdam, Fatemeh, additional, Cavallaro, Paul M., additional, Hamarneh, Sulaiman R., additional, Tsurumi, Amy, additional, Hoda, Raza S., additional, Munoz, Alexander R., additional, Dhole, Yashoda, additional, Ramirez, Juan M., additional, Liu, Enyu, additional, Vasan, Robin, additional, Liu, Yang, additional, Samarbafzadeh, Ehsan, additional, Nunez, Rocio A., additional, Farber, Matthew Z., additional, Chopra, Vanita, additional, Malo, Madhu S., additional, Rahme, Laurence G., additional, and Hodin, Richard A., additional

Published
2020
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16. Targeted gene walking by low stringency polymerase chain reaction: assignment of a putative human brain sodium channel gene (SCN3A) to chromosome 2q24-31

Author

Malo, Madhu S., Srivastava, Kakul, Andresen, Joshua M., Chen, Xiao-Ning, Korenberg, Julie R., and Ingram, Vernon M.

Subjects
DNA sequencers -- Research, Polymerase chain reaction -- Analysis, Sodium channels -- Genetic aspects, Science and technology
Abstract

Facile targeted gene walking is facilitated by a low stringency polymerase chain reaction, LSPCR, designed to isolate the unknown site surrounding a known DNA sequence. SCN3A, a putative human brain sodium channel gene, was assigned to chromosome 2q24-31.

Published
1994

19. The intestinal epithelial cell differentiation marker intestinal alkaline phosphatase (ALPi) is selectively induced by histone deacetylase inhibitors (HDACi) in colon cancer cells in a Kruppel-like factor 5 (KLF5)-dependent manner.

Author

Shin, Joongho, primary, Carr, Azadeh, additional, Corner, Georgia A., additional, Tögel, Lars, additional, Dávalos-Salas, Mercedes, additional, Tran, Hoanh, additional, Chueh, Anderly C., additional, Al-Obaidi, Sheren, additional, Chionh, Fiona, additional, Ahmed, Naseem, additional, Buchanan, Daniel D., additional, Young, Joanne P., additional, Malo, Madhu S., additional, Hodin, Richard A., additional, Arango, Diego, additional, Sieber, Oliver M., additional, Augenlicht, Leonard H., additional, Dhillon, Amardeep S., additional, Weber, Thomas K., additional, and Mariadason, John M., additional

Published
2015
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20. A Novel Approach to Maintain Gut Mucosal Integrity Using an Oral Enzyme Supplement

Author

Hamarneh, Sulaiman R., primary, Mohamed, Mussa M. Rafat, additional, Economopoulos, Konstantinos P., additional, Morrison, Sara A., additional, Phupitakphol, Tanit, additional, Tantillo, Tyler J., additional, Gul, Sarah S., additional, Gharedaghi, Mohammad Hadi, additional, Tao, Qingsong, additional, Kaliannan, Kanakaraju, additional, Narisawa, Sonoko, additional, Millán, José L., additional, van der Wilden, Gwendolyn M., additional, Fagenholz, Peter J., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2014
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21. The Intestinal Epithelial Cell Differentiation Marker Intestinal Alkaline Phosphatase (ALPi) Is Selectively Induced by Histone Deacetylase Inhibitors (HDACi) in Colon Cancer Cells in a Kruppel-like Factor 5 (KLF5)-dependent Manner

Author

Shin, Joongho, primary, Carr, Azadeh, additional, Corner, Georgia A., additional, Tögel, Lars, additional, Dávaos-Salas, Mercedes, additional, Tran, Hoanh, additional, Chueh, Anderly C., additional, Al-Obaidi, Sheren, additional, Chionh, Fiona, additional, Ahmed, Naseem, additional, Buchanan, Daniel D., additional, Young, Joanne P., additional, Malo, Madhu S., additional, Hodin, Richard A., additional, Arango, Diego, additional, Sieber, Oliver M., additional, Augenlicht, Leonard H., additional, Dhillon, Amardeep S., additional, Weber, Thomas K., additional, and Mariadason, John M., additional

Published
2014
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22. Intestinal alkaline phosphatase promotes gut bacterial growth by reducing the concentration of luminal nucleotide triphosphates

Author

Malo, Madhu S., primary, Moaven, Omeed, additional, Muhammad, Nur, additional, Biswas, Brishti, additional, Alam, Sayeda N., additional, Economopoulos, Konstantinos P., additional, Gul, Sarah Shireen, additional, Hamarneh, Sulaiman R., additional, Malo, Nondita S., additional, Teshager, Abeba, additional, Mohamed, Mussa M. Rafat, additional, Tao, Qingsong, additional, Narisawa, Sonoko, additional, Millán, José Luis, additional, Hohmann, Elizabeth L., additional, Warren, H. Shaw, additional, Robson, Simon C., additional, and Hodin, Richard A., additional

Published
2014
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23. Intestinal Alkaline Phosphatase Prevents Antibiotic-Induced Susceptibility to Enteric Pathogens

Author

Alam, Sayeda Nasrin, primary, Yammine, Halim, additional, Moaven, Omeed, additional, Ahmed, Rizwan, additional, Moss, Angela K., additional, Biswas, Brishti, additional, Muhammad, Nur, additional, Biswas, Rakesh, additional, Raychowdhury, Atri, additional, Kaliannan, Kanakaraju, additional, Ghosh, Sathi, additional, Ray, Madhury, additional, Hamarneh, Sulaiman R., additional, Barua, Soumik, additional, Malo, Nondita S., additional, Bhan, Atul K., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2014
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26. Tu1620 Intestinal Alkaline Phosphatase Is an Endogenous Anti-Inflammatory Factor

Author

Mohamed, Mussa, primary, Economopoulos, Konstantinos P., additional, Patel, Palak, additional, Muhammad, Nur, additional, Moaven, Omeed, additional, Moss, Angela K., additional, Hamarneh, Sulaiman R., additional, Teshager, Abeba, additional, Kaliannan, Kanakaraju, additional, Abtahi, Seyed M., additional, Alam, Sayeda Nasrin, additional, Malo, Nondita S., additional, Tao, Qingsong, additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2013
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28. Abstract 2991: Coordinate methylation of the alkaline phosphatase gene family in colon cancer. Implications for understanding the manifestation of the CpG island methylator phenotype (CIMP). .

Author

Mariadason, John, primary, Carr, Azadeh, additional, Corner, Georgia A., additional, Al-Obaidi, Sheren, additional, Chueh, Anderly, additional, Chionh, Fiona, additional, Tögel, Lars, additional, Ahmed, Naseem, additional, Arango, Diego, additional, Buchanan, Daniel, additional, Young, Joanne, additional, Augenlicht, Leonard H., additional, Malo, Madhu S., additional, Hodin, Richard, additional, Sieber, Oliver M., additional, Weber, Thomas, additional, and Shin, Joongho, additional

Published
2013
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29. Intestinal alkaline phosphatase inhibits the proinflammatory nucleotide uridine diphosphate

Author

Moss, Angela K., primary, Hamarneh, Sulaiman R., additional, Mohamed, Mussa M. Rafat, additional, Ramasamy, Sundaram, additional, Yammine, Halim, additional, Patel, Palak, additional, Kaliannan, Kanakaraju, additional, Alam, Sayeda N., additional, Muhammad, Nur, additional, Moaven, Omeed, additional, Teshager, Abeba, additional, Malo, Nondita S., additional, Narisawa, Sonoko, additional, Millán, José Luis, additional, Warren, H. Shaw, additional, Hohmann, Elizabeth, additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2013
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31. 632 Prevention of Antibiotic-Associated DSS Colitis by Intestinal Alkaline Phosphatase

Author

Ahmed, Rizwan, primary, Alam, Sayeda Nasrin, additional, Economopoulos, Konstantinos P., additional, Moaven, Omeed, additional, Ray, Madhury, additional, Kaliannan, Kanakaraju, additional, Hamarneh, Sulaiman R., additional, Muhammad, Nur, additional, Barua, Soumik, additional, Raychowdhury, Atri, additional, Mohamed, Mussa, additional, Bhan, Atul K., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2012
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32. Sa2066 A Novel Function of Intestinal Alkaline Phosphatase as an Endogenous Prebiotic

Author

Moaven, Omeed, primary, Alam, Sayeda Nasrin, additional, Ray, Madhury, additional, Kaliannan, Kanakaraju, additional, Ahmed, Rizwan, additional, Hamarneh, Sulaiman R., additional, Economopoulos, Konstantinos P., additional, Moss, Angela K., additional, Muhammad, Nur, additional, Mohamed, Mussa, additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2012
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34. Mo1177 The Effects of Orally Administered Intestinal Alkaline Phosphatase on High-Fat Diet-Induced Metabolic Disorders

Author

Kaliannan, Kanakaraju, primary, Alam, Sayeda Nasrin, additional, Moaven, Omeed, additional, Moss, Angela K., additional, Ray, Madhury, additional, Ahmed, Rizwan, additional, Hamarneh, Sulaiman R., additional, Muhammad, Nur, additional, Economopoulos, Konstantinos P., additional, Mohamed, Mussa, additional, Bhan, Atul K., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2012
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35. Mo1820 Oral Supplementation With Intestinal Alkaline Phosphatase: A Novel Therapy to Treat Salmonella Colitis

Author

Alam, Sayeda Nasrin, primary, Yammine, Halim, additional, Ahmed, Rizwan, additional, Hamarneh, Sulaiman R., additional, Economopoulos, Konstantinos P., additional, Moaven, Omeed, additional, Kaliannan, Kanakaraju, additional, Moss, Angela K., additional, Ray, Madhury, additional, Muhammad, Nur, additional, Mohamed, Mussa, additional, Raychowdhury, Atri, additional, Barua, Soumik, additional, Bhan, Atul K., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2012
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36. ATP-Induced Activation of NLRP3 Inflammasome and IL-1β Secretion Prevented by Intestinal Alkaline Phosphatase

Author

Ramasamy, Sundaram, primary, Malo, Madhu S., additional, Nasrin Alam, Sayeda, additional, Yammine, Halim, additional, Kaliannan, Kanakaraju, additional, Moss, Angela K., additional, Muhammad, Nur, additional, Biswas, Rakesh, additional, Batal, Obaida H., additional, Raychowdhury, Atri, additional, Warren, H. Shaw, additional, Hohmann, Elizabeth, additional, Bhan, Atul K., additional, and Hodin, Richard A., additional

Published
2011
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37. Intestinal Alkaline Phosphatase Detoxifies Bacterial Components

Author

Moss, Angela K., primary, Malo, Madhu S., additional, Yammine, Halim, additional, Nasrin Alam, Sayeda, additional, Ramasamy, Sundaram, additional, Biswas, Rakesh, additional, Muhammad, Nur, additional, Kaliannan, Kanakaraju, additional, Batal, Obaida H., additional, Warren, H. Shaw, additional, Hohmann, Elizabeth, additional, and Hodin, Richard A., additional

Published
2011
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38. Intestinal alkaline phosphatase has beneficial effects in mouse models of chronic colitis

Author

Ramasamy, Sundaram, primary, Nguyen, Deanna D., additional, Eston, Michelle A., additional, Nasrin Alam, Sayeda, additional, Moss, Angela K., additional, Ebrahimi, Farzad, additional, Biswas, Brishti, additional, Mostafa, Golam, additional, Chen, Kathryn T., additional, Kaliannan, Kanakaraju, additional, Yammine, Halim, additional, Narisawa, Sonoko, additional, Millán, José Luis, additional, Warren, Shaw H., additional, Hohmann, Elizabeth L., additional, Mizoguchi, Emiko, additional, Reinecker, Hans-Christian, additional, Bhan, Atul K., additional, Snapper, Scott B., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2011
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40. M1736 Intestinal Alkaline Phosphatase has Beneficial Effects in Mouse Models of Chronic Colitis

Author

Ramasamy, Sundaram, primary, Nguyen, Deanna D., additional, Eston, Michelle A., additional, Mostafa, Golam, additional, Muhammad, Nur, additional, Ebrahimi, Farzad, additional, Alam, Sayeda Nasrin, additional, Chen, Kathryn, additional, Biswas, Brishti, additional, Moss, Angela K., additional, Yammine, Halim, additional, Narisawa, Sonoko, additional, Millan, Jose L., additional, Shaw, Warren H., additional, Hohmann, Elizabeth, additional, Mizoguchi, Emiko, additional, Reinecker, Hans-Christian, additional, Bhan, Atul K., additional, Snapper, Scott B., additional, Malo, Madhu S., additional, and Hodin, Richard A., additional

Published
2010
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41. W1825 Intestinal Alkaline Phosphatase to Treat and Prevent Enteric Bacterial Pathogenesis

Author

Malo, Madhu S., primary, Mostafa, Golam, additional, Muhammad, Nur, additional, Ebrahimi, Farzad, additional, Alam, Sayeda Nasrin, additional, Chen, Kathryn, additional, Ramasamy, Sundaram, additional, Biswas, Brishti, additional, Moss, Angela K., additional, Yammine, Halim, additional, Shaw, Warren H., additional, Hohmann, Elizabeth, additional, and Hodin, Richard A., additional

Published
2010
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42. W1770 Thyroid Hormone Modulates the Normal Homeostasis of Intestinal Microbiota

Author

Alam, Sayeda Nasrin, primary, Malo, Madhu S., additional, Ebrahimi, Farzad, additional, Mostafa, Golam, additional, Chen, Kathryn, additional, Ramasamy, Sundaram, additional, Muhammad, Nur, additional, Biswas, Brishti, additional, Yammine, Halim, additional, Moss, Angela K., additional, Shaw, Warren H., additional, Hohmann, Elizabeth, additional, and Hodin, Richard A., additional

Published
2010
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43. W1866 Local Peritoneal Irrigation With Intestinal Alkaline Phosphatase is Protective Against Peritonitis in Mice

Author

Ebrahimi, Farzad, primary, Malo, Madhu S., additional, Alam, Sayeda Nasrin, additional, Chen, Kathryn, additional, Mostafa, Golam, additional, Ramasamy, Sundaram, additional, Moss, Angela K., additional, Biswas, Brishti, additional, Yammine, Halim, additional, Shaw, Warren H., additional, Hohmann, Elizabeth, additional, and Hodin, Richard A., additional

Published
2010
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