Priya Prahalad, MD

  • Priya Prahalad



Trabajo y Educación

Formación Profesional

Georgetown University School of Medicine, Washington, DC, 5/23/2010


University of California San Francisco Internal Medicine Residency, San Francisco, CA, 6/30/2011


University of California San Francisco Internal Medicine Residency, San Francisco, CA, 6/30/2012


University of California San Francisco Internal Medicine Residency, San Francisco, CA, 6/30/2015

Certificaciones Médicas

Pediatric Endocrinology, American Board of Pediatrics

Pediatrics, American Board of Pediatrics



Todo Publicaciones

Diabetes technology: improving care, improving patient-reported outcomes and preventing complications in young people with Type 1 diabetes. Diabetic medicine : a journal of the British Diabetic Association Prahalad, P., Tanenbaum, M., Hood, K., Maahs, D. M. 2018


With the evolution of diabetes technology, those living with Type 1 diabetes are given a wider arsenal of tools with which to achieve glycaemic control and improve patient-reported outcomes. Furthermore, the use of these technologies may help reduce the risk of acute complications, such as severe hypoglycaemia and diabetic ketoacidosis, as well as long-term macro- and microvascular complications. In addition, diabetes technology can have a beneficial impact on psychosocial health by reducing the burden of diabetes. Unfortunately, diabetes goals are often unmet and people with Type 1 diabetes too frequently experience acute and long-term complications of this condition, in addition to often having less than ideal psychosocial outcomes. Increasing realization of the importance of patient-reported outcomes is leading to diabetes care delivery becoming more patient-centred. Diabetes technology in the form of medical devices, digital health and big data analytics have the potential to improve clinical care and psychosocial support, resulting in lower rates of acute and chronic complications, decreased burden of diabetes care, and improved quality of life. This article is protected by copyright. All rights reserved.

View details for DOI 10.1111/dme.13588

View details for PubMedID 29356074

Evidence-based Mobile Medical Applications in Diabetes. Endocrinology and metabolism clinics of North America Drincic, A., Prahalad, P., Greenwood, D., Klonoff, D. C. 2016; 45 (4): 943-965


This article reviews mobile medical applications that are commercially available in the United States or European Union (EU) and are (1) associated with published data of clinical outcomes in the peer-reviewed literature during the past 5 years, (2) cleared by the US Food and Drug Administration (FDA) in the United States, or (3) a recipient of a CE (Conformit Europenne) mark by the EU. Many of these applications have been shown to positively affect outcomes in the short term, but long-term studies are needed. Until more data are available, consumers and professionals can consider guidance based on FDA/CE status.

View details for DOI 10.1016/j.ecl.2016.06.001

View details for PubMedID 27823614

Performance of Cleared Blood Glucose Monitors. Journal of diabetes science and technology Klonoff, D. C., Prahalad, P. 2015; 9 (4): 895-910


Cleared blood glucose monitor (BGM) systems do not always perform as accurately for users as they did to become cleared. We performed a literature review of recent publications between 2010 and 2014 that present data about the frequency of inaccurate performance using ISO 15197 2003 and ISO 15197 2013 as target standards. We performed an additional literature review of publications that present data about the clinical and economic risks of inaccurate BGMs for making treatment decisions or calibrating continuous glucose monitors (CGMs). We found 11 publications describing performance of 98 unique BGM systems. 53 of these 98 (54%) systems met ISO 15197 2003 and 31 of the 98 (32%) tested systems met ISO 15197 2013 analytical accuracy standards in all studies in which they were evaluated. Of the tested systems, 33 were identified by us as FDA-cleared. Among these FDA-cleared BGM systems, 24 out of 32 (75%) met ISO 15197 2003 and 15 out of 31 (48.3%) met ISO 15197 2013 in all studies in which they were evaluated. Among the non-FDA-cleared BGM systems, 29 of 65 (45%) met ISO 15197 2003 and 15 out of 65 (23%) met ISO 15197 2013 in all studies in which they were evaluated. It is more likely that an FDA-cleared BGM system, compared to a non-FDA-cleared BGM system, will perform according to ISO 15197 2003 ((2) = 6.2, df = 3, P = 0.04) and ISO 15197 2013 ((2) = 11.4, df = 3, P = 0.003). We identified 7 articles about clinical risks and 3 articles about economic risks of inaccurate BGMs. We conclude that a significant proportion of cleared BGMs do not perform at the level for which they were cleared or according to international standards of accuracy. Such poor performance leads to adverse clinical and economic consequences.

View details for DOI 10.1177/1932296815584797

View details for PubMedID 25990294

Retinoic acid mediates regulation of network formation by COUP-TFII and VE-cadherin expression by TGFbeta receptor kinase in breast cancer cells. PloS one Prahalad, P., Dakshanamurthy, S., Ressom, H., Byers, S. W. 2010; 5 (4)


Tumor development, growth, and metastasis depend on the provision of an adequate vascular supply. This can be due to regulated angiogenesis, recruitment of circulating endothelial progenitors, and/or vascular transdifferentiation. Our previous studies showed that retinoic acid (RA) treatment converts a subset of breast cancer cells into cells with significant endothelial genotypic and phenotypic elements including marked induction of VE-cadherin, which was responsible for some but not all morphological changes. The present study demonstrates that of the endothelial-related genes induced by RA treatment, only a few were affected by knockdown of VE-cadherin, ruling it out as a regulator of the RA-induced endothelial genotypic switch. In contrast, knockdown of the RA-induced gene COUP-TFII prevented the formation of networks in Matrigel but had no effect on VE-cadherin induction or cell fusion. Two pan-kinase inhibitors markedly blocked RA-induced VE-cadherin expression and cell fusion. However, RA treatment resulted in a marked and broad reduction in tyrosine kinase activity. Several genes in the TGFbeta signaling pathway were induced by RA, and specific inhibition of the TGFbeta type I receptor blocked both RA-induced VE-cadherin expression and cell fusion. Together these data indicate a role for the TGFbeta pathway and COUP-TFII in mediating the endothelial transdifferentiating properties of RA.

View details for DOI 10.1371/journal.pone.0010023

View details for PubMedID 20386594

Role of Sox-9, ER81 and VE-Cadherin in Retinoic Acid-Mediated Trans-Differentiation of Breast Cancer Cells PLOS ONE Endo, Y., Deonauth, K., Prahalad, P., Hoxter, B., Zhu, Y., Byers, S. W. 2008; 3 (7)


Many aspects of development, tumor growth and metastasis depend upon the provision of an adequate vasculature. This can be a result of regulated angiogenesis, recruitment of circulating endothelial progenitors and/or vascular trans-differentiation. The present study demonstrates that treatment of SKBR-3 breast cancer cells with retinoic acid (RA), an important regulator of embryogenesis, cancer and other diseases, stimulates the formation of networks in Matrigel. RA-treatment of SKBR-3 cells co-cultured with human umbilical vein endothelial cells resulted in the formation of mixed structures. RA induces expression of many endothelial genes including vascular endothelial (VE) cadherin. VE-cadherin was also induced by RA in a number of other breast cancer cells. We show that RA-induced VE-cadherin is responsible for the RA-induced morphological changes. RA rapidly induced the expression of Sox-9 and ER81, which in turn form a complex on the VE-cadherin promoter and are required to mediate the transcriptional regulation of VE-cadherin by RA. These data indicate that RA may promote the expression of endothelial genes resulting in endothelial-like differentiation, or provide a mechanism whereby circulating endothelial progenitor cells could be incorporated into a growing organ or tumor.

View details for DOI 10.1371/journal.pone.0002714

View details for Web of Science ID 000264057200057

View details for PubMedID 18628953

Regulation of MDCK cell-substratum adhesion by RhoA and myosin light chain kinase after ATP depletion AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY Prahalad, P., Calvo, I., Waechter, H., Matthews, J. B., Zuk, A., Matlin, K. S. 2004; 286 (3): C693-C707


The attachment of epithelial cells to the extracellular matrix substratum is essential for their differentiation and polarization. Despite this, the precise adhesion mechanism and its regulation are poorly understood. In the kidney, an ischemic insult causes renal tubular epithelial cells to detach from the basement membrane, even though they remain viable. To understand this phenomenon, and to probe the regulation of epithelial cell attachment, we used a model system consisting of newly adherent Madin-Darby canine kidney (MDCK) cells subjected to ATP depletion to mimic ischemic injury. We found that MDCK cells detach from collagen I after 60 min of ATP depletion but reattach when resupplied with glucose. Detachment is not caused by degradation or endocytosis of beta(1)-integrins, which mediate attachment to collagen I. Basal actin filaments and paxillin-containing adhesion complexes are disrupted by ATP depletion and quickly reform on glucose repletion. However, partial preservation of basal actin by overexpression of constitutively active RhoA does not significantly affect cell detachment. Furthermore, Y-27632, an inhibitor of the RhoA effector Rho-kinase, does not prevent reattachment of cells on glucose addition, even though reformation of central stress fibers and large adhesion complexes is blocked. In contrast, reattachment of ATP-depleted cells and detachment of cells not previously subjected to ATP depletion are prevented by ML-7, an inhibitor of myosin light chain kinase (MLCK). We conclude that initial adherence of MDCK cells to a collagen I substratum is mediated by peripheral actin filaments and adhesion complexes regulated by MLCK but not by stress fibers and adhesion complexes controlled by RhoA.

View details for DOI 10.1152/ajpcell.00124.2003

View details for Web of Science ID 000188707600027

View details for PubMedID 14644769