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Kandimalla, Karunya K.

https://orcid.org/0000-0001-7786-1915

Mayo Clinic

University of Minnesota

Citations 33

Gut Microbiota Alter Colonic Expression of Genes Encoding Drug Transporters and Drug-Metabolizing Enzymes in Mice
Nelson, D. , Veerareddy, Vaishnavi, Tang, Xiaojiao, Kashyap, Purna C., Kalari, Krishna R., Kandimalla, Karunya K. , Kandimalla, Karunya K , Kashyap, Purna

International Journal of Molecular Sciences | August 24, 2026 | Volume: 27 | Issue: 17 | Pages: 7583

10.3390/ijms27177583 Get It

Gut microbiota regulate the intestinal expression of drug-metabolizing enzymes, transporters, and barrier properties that determine oral drug absorption and disposition. This study compares germ-free Swiss Webster mice to mice colonized with fecal microbiota from a single human donor, evaluating microbiota-driven differences in colonic gene expression and P-gp protein expression, as well as small intestinal mucosal permeability. Transcriptomic analysis of colonic tissue revealed microbiota-induced upregulation of genes encoding P-gp and other drug transporters, including MCT1 and OCTN2. Immunofluorescence also indicated greater P-gp expression and apical localization in colonized mice. Gene expression of drug-metabolizing enzymes was also higher in colonized mice, including phase I enzymes (carboxylesterase 2 paralogs), phase II enzymes (UDP-glucuronosyltransferases and glutathione S-transferases), and enzymes responsible for synthesizing their co-substrates, UDP-glucuronic acid and glutathione. Small intestinal mucosal explants demonstrated lower permeability to 14C-labeled polyethylene glycol 4000 in colonized mice compared to germ-free mice. In the colon, transcriptomic analysis identified microbiota-dependent changes in genes regulating paracellular tight junctions and actomyosin contractility. These results show that human-derived gut microbiota alter gene expression in the mouse colon, identifying candidate microbiota-responsive genes relevant to oral drug absorption and disposition.
Disruptions in glucose and amyloid-beta transport in mouse models manifesting metabolic syndrome
Wang, Lushan , Curran, Geoffry L., Gali, Chaitanya Chakravarthi , Zhou, Andrew L, Min, Paul Hu, Lowe, Val J. , Zhou, Andrew L., Min, Paul H., Kandimalla, Karunya K.

No container title available | August 20, 2026 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.64898/2026.08.15.741912 Get It

ABSTRACT Studies in humans and murine models have pointed towards a possible link between metabolic syndrome, which shows insulin resistance and metabolic dysregulation, and Alzheimer’s disease (AD) pathology marked by amyloid-beta (Aβ) accumulation at the BBB and hypometabolism in the brain. Yet, the underlying biological mechanisms by which metabolic syndrome affects these pathological changes in AD brain remain unknown. We hypothesized that insulin resistance is responsible for alterations in blood-brain barrier (BBB) transport of Aβ peptides and glucose. This hypothesis was tested by employing radiolabeled tracers ( 125 I-Aβ40, 125 I-Aβ42, and 18 F-FDG) in high-fat diet (HFD)-fed mouse models that manifest metabolic syndrome. Further, we assessed alterations in the expression of various molecular mediators within the brain microcapillaries harvested from both low-fat diet (LFD)-fed and HFD-fed mice. As expected, our studies show that HFD- fed mice developed peripheral insulin resistance and obesity. In addition, HFD-fed mice demonstrated an increase in the influx rate of Aβ peptides and a reduction in 18 F-FDG (a glucose surrogate) influx rate at the BBB compared to LFD-fed mice. These transport changes are associated with increase in the BBB endothelial expression of RAGE (receptor to traffic Aβ from plasma-to-brain) and a reduction of GLUT1 (glucose transporter) expression in HFD-fed mice compared to LFD-fed mice. Moreover, disruption in insulin signaling, as indicated by reduced pAKT and pERK expression, was observed in HFD-fed mice. Inhibiting AKT or ERK phosphorylation with specific inhibitors resulted in similar changes in Aβ and glucose uptake in polarized BBB endothelial cell monolayers in vitro. These results indicate that HFD induced metabolic syndrome may lead to BBB dysfunction, characterized by increased plasma-to-brain Aβ trafficking and diminished glucose transport at the BBB, thereby aggravating the expression of AD pathological hallmarks.
Neurophysiological mechanisms of breathing-based well-being practices: a narrative review for clinical application
Veerareddy, Vaishnavi, 홍이수, Nycklemoe, Marin, Kandimalla, Mahathi, Sharma, Vamika, Kung, Tiffany L., Osman, Rowa, Min, Paul H., Hong, Isu, Sharma, Pravesh , Veerareddy, Vaishnavi, Nycklemoe, Marin, Kung, Tiffany L., Lim, Seokbeen , Kandimalla, Karunya K. , Lapid, Maria I.

Frontiers in Psychiatry | July 8, 2026 | Volume: 17 | Issue: No issue available | Pages: No page available

10.3389/fpsyt.2026.1774490 Get It

Breathing is a physiological process that extends beyond gas exchange, linking neural, cardiovascular, glymphatic, and autonomic systems. This narrative review summarizes how breathing-based practices modulate physiological processes in the body and brain, emphasizing their applicability in clinical care. Regulating the pace and depth of breathing, particularly with relaxed exhalation, may engage vagal pathways that lower heart rate and blood pressure and promote a shift toward increased parasympathetic tone relative to sympathetic activity. Neuroimaging studies show that controlled breathing reduces activity in stress-related brain regions while enhancing networks supporting calm attention and emotional steadiness. Changes in breathing depth also influence cerebrospinal fluid movement, though direct evidence of waste clearance in humans is lacking. This review identifies populations requiring caution, including individuals with panic symptoms, significant cardiopulmonary disease, or pregnancy. Clinicians should distinguish between breathing-only and multimodal protocols when interpreting research findings, as combined interventions preclude attribution of benefit to breathing alone. Study design quality, particularly the use of active rather than waitlist controls, should inform how effect sizes are interpreted. Breathing practices are not a replacement for medical treatment but may represent accessible, low-cost adjuncts for stress reduction and cardiovascular regulation.
Butyrate Regulates the Blood–Brain Barrier Transport and Intraendothelial Accumulation of Alzheimer’s Disease Amyloid-Beta Peptides
Veerareddy, Vaishnavi, Kashyap, Purna , Kandimalla, Karunya K. , Kandimalla, Karunya K , Wang, Zengtao

Molecular Pharmaceutics | May 21, 2026 | Volume: 23 | Issue: 7 | Pages: 3529-3540

10.1021/acs.molpharmaceut.5c01594 Get It

Estimation of Various Physiological Parameters Affecting Amyloid Plaque Distribution of a Novel MRI Contrast Agent in the Brain of Alzheimer’s Disease Transgenic Mice
Salian, Vrishali S. , Curran, Geoffry, Podulso, Joseph F., Kandimalla, Karunya K. , Salian, Vrishali , Kandimalla, Karunya K , Wang, Zengtao , Curran, Geoffry L.

Molecular Pharmaceutics | May 5, 2026 | Volume: 23 | Issue: 6 | Pages: 3243-3253

10.1021/acs.molpharmaceut.5c01565 Get It

Acute amyloid-β exposure disrupts insulin signaling in blood–brain barrier endothelial cell culture models
Nelson, D. , Swaminathan, Suresh Kumar, Seo, Hannah S., Azarin, Samira M. , Veerareddy, Vaishnavi, Azarin, Samira M. , Kalari, Krishna R., Kandimalla, Karunya K.

No container title available | January 12, 2026 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.21203/rs.3.rs-8436616/v1 Get It

Abstract Background Brain insulin resistance and cerebrovascular dysfunction emerge early in late-onset Alzheimer’s disease, but how amyloid-β (Aβ) disrupts insulin signaling at the cerebrovascular blood–brain barrier—a major site of insulin receptor signaling and transport into the brain—remains unclear. Methods We exposed two distinct human blood-brain-barrier endothelial cell models to soluble Aβ40 or Aβ42 for 1 h, followed by 100 nM insulin for 10 min. Protein and phosphoprotein responses were quantified by reverse-phase protein array, and differential expression was evaluated using linear models. Results Aβ40 reduced insulin-stimulated Akt activation and converted insulin’s normal inhibition of AMPK into modest stimulation. Aβ42 did not alter insulin-stimulated Akt signaling but moderately suppressed basal Akt activation. Conclusions These findings suggest that Aβ40 acutely impairs insulin signal transduction in BBB endothelial cells, supporting a model in which vascular Aβ exposure contributes directly to the early development of brain insulin resistance in AD.
Amyloid beta peptides inhibit glucose transport at the blood-brain barrier by disrupting the insulin-AKT pathway
Wang, Lushan , Curran, Geoffry L., Zhong, Rui , Zheng, Xue , Veerareddy, Vaishnavi, Thieschafer, Josslen S., Min, Hoon‐Ki , Lowe, Val J. , Kandimalla, Karunya K. , Kandimalla, Karunya K , Min, Hoon-Ki Paul , Xue, Zheng, Li, Ling

Journal of Cerebral Blood Flow & Metabolism | May 15, 2025 | Volume: 45 | Issue: 10 | Pages: 1961-1979

10.1177/0271678x251332493 Get It

Abstract Molecular mechanisms underlying disruptions in brain glucose uptake and metabolism, linked with cognitive decline in Alzheimer’s disease (AD) patients, are only partially understood. This study investigated how soluble amyloid beta (sAβ) peptides affect glucose transport at the blood-brain barrier (BBB), the primary portal for glucose entry into the brain. We demonstrated that [ 18 F]-fluorodeoxyglucose ( 18 FDG) uptake is reduced in sAβ overproducing APP,PS1 transgenic mice compared to wild-type mice. Moreover, the influx rate of 18 FDG decreased in sAβ40 or sAβ42 pre-infused mice, highlighting the inhibitory effect of sAβ peptides on glucose transport at the BBB. Consistently, the expression of GLUT1, the primary glucose transporter at the BBB, is reduced in polarized human cerebral microvascular endothelial cell (hCMEC/D3) monolayers upon exposure to sAβ peptides and in Aβ-laden cerebral vasculature in vivo. The study further examined the influence of sAβ on the insulin-AKT pathway, known to regulate glucose uptake through modulation of thioredoxin-interacting protein (TXNIP) expression. Results showed that sAβ peptides suppress AKT phosphorylation and reduce GLUT1 expression by upregulating TXNIP levels in hCMEC/D3 monolayers. Co-incubation of resveratrol with sAβ peptides reduced TXNIP expression and rectified reductions in GLUT1 expression. In summary, toxic sAβ impairs BBB glucose transport by disrupting the insulin/AKT/TXNIP axis.
Characterization of transcriptomic changes in the neurovascular unit of Alzheimiers transgenic mouse models using digital spatial profiling
Salian, Vrishali S. , Lowe, Val J. , Salian, Vrishali , Thompson, Kevin J. , Tang, Xiaojia , Kalari, Krishna R. , Kandimalla, Karunya K.

No container title available | March 11, 2025 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.1101/2025.03.03.640886 Get It

Abstract Alzheimer’s disease (AD) affects 40 million individuals globally and is characterized by the accumulation of amyloid-beta (Aβ) proteins, which aggregate and form plaques. BBB dysfunction drives AD cerebrovascular pathology and BBB integrity is maintained by neurovascular unit (NVU). Specifically, within the NVU, the cerebral endothelial cells maintain vascular homeostasis. In this study, we isolated endothelial-enriched regions of interest (ROIs) using the Nanostring GeoMx digital spatial profiler and employed a deconvolution model to evaluate transcriptomic changes. We observed dysregulation of cellular signaling potentially disrupting the APP+ BBB integrity. Analysis of ligand-receptor pairings that are the foundation of the NVU intercellular signaling indicated that the endothelial vasculature completes a feedback loop with the NVU to the regulating astroctyes. Further, we identified potentially antagonistic signaling roles for opioid receptor species that should be further investigated for potential therapeutic targets. Graphical Abstract
Elucidating Molecular Mechanisms Governing TNF-Alpha-Mediated Regulation of Amyloid Beta 42 Uptake in Blood-Brain Barrier Endothelial Cells
Salian, Vrishali S. , Curan, Geoffry L., Lowe, Val J. , Tang, Xiaojia , Salian, Vrishali , Kalari, Krishna R. , Kandimalla, Karunya K.

No container title available | January 29, 2025 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.1101/2025.01.28.635286 Get It

Abstract Cerebrovascular inflammation is prevalent in a majority of Alzheimer’s patients. Inflammatory cytokines, such as tumor necrosis factor-alpha (TNF-alpha), circulating in the plasma have been shown to cause the inflammation of blood-brain barrier (BBB) endothelium lining the cerebral microvasculature. The BBB inflammation has been implicated in the increase of toxic Aβ accumulation within Alzheimer’s disease (AD) brain. TNF-alpha in the peripheral circulation can aggravate the accumulation of amyloid-beta (Aβ) peptides in Alzheimer’s disease brain. In the current study, we have shown that the exposure to TNF-alpha leads to an increase in Aβ42 accumulation in mice and BBB endothelial cells in vitro. Moreover, dynamic SPECT/CT imaging in wild-type (WT) mice infused with TNF-alpha increased the permeability and influx of Aβ42 into the mice brain. In addition, our results show that TNF-alpha modifies the expression of cofilin, actin, and dynamin, which are critical components for Aβ endocytosis by BBB endothelial cells. These results offer a mechanistic understanding of how TNF-alpha may promote Aβ accumulation at the BBB and the underlying interactions between inflammation and Aβ exposure that drives BBB dysfunction. Hence, a therapeutic intervention aimed at addressing cerebrovascular inflammation in Alzheimer’s disease may potentially reduce Aβ induced cerebrovascular toxicity in Alzheimer’s disease brain. Significance statement Increased levels of TNF-alpha circulating in the plasma are considered significant factors in the consequences of Aβ pathology in Alzheimer’s disease, where it can promote cerebrovascular inflammation and BBB dysfunction. However, the role of TNF-alpha, in exacerbating Aβ pathology by increasing Aβ accumulation at the BBB endothelial cells remains only partially understood. In this study, we demonstrated that TNF-alpha enhances Aβ42 accumulation in the BBB endothelium by altering the expression of the BBB endocytosis machinery, specifically cofilin, actin, and dynamin. These findings are anticipated to contribute to the development of therapeutic approaches aimed at addressing elevated cytokine levels in Alzheimer’s disease. Graphical Abstract
QSP Modeling Shows Pathological Synergism Between Insulin Resistance and Amyloid‐Beta Exposure in Upregulating VCAM1 Expression at the BBB Endothelium
Wang, Zengtao , Veerareddy, Vaishnavi, Tang, Xiao-Jiao, Thompson, Kevin J. , Krishnan, Sunil , Kandimalla, Karunya K. , Tang, Xiaojiao, Kalari, Krishna R , Kandimalla, Karunya K , Krishnan, Sunil , Thompson, Kevin J , Tang, Xiaojiao, Kalari, Krishna R.

CPT: Pharmacometrics & Systems Pharmacology | December 27, 2024 | Volume: 14 | Issue: 3 | Pages: 561-571

10.1002/psp4.13296 Get It

ABSTRACTType 2 diabetes mellitus (T2DM), characterized by insulin resistance, is closely associated with Alzheimer's disease (AD). Cerebrovascular dysfunction is manifested in both T2DM and AD, and is often considered as a pathological link between the two diseases. Insulin signaling regulates critical functions of the blood–brain barrier (BBB), and endothelial insulin resistance could lead to BBB dysfunction, aggravating AD pathology. However, insulin signaling is intrinsically dynamic and involves interactions among numerous molecular mediators. Hence, a mechanistic systems biology model is needed to understand how insulin regulates BBB physiology and the consequences of its impairment in T2DM and AD. In this study, we investigated the pharmacodynamic effect of insulin on the expression of vascular cell adhesion molecule 1 (VCAM1), a marker of cerebrovascular inflammation. Intriguingly, normal insulin concentrations selectively activated the PI3K‐AKT pathway, leading to decreased VCAM1 expression. However, exposure to supraphysiological insulin levels, which is present in insulin resistance, activated both PI3K‐AKT and MEK–ERK pathways, and increased VCAM1 expression. We developed a mathematical model that adequately described the dynamics of various insulin signaling nodes and VCAM1 expression. Further, the model was integrated with in vitro proteomics and transcriptomics data from AD patients to simulate VCAM1 expression under pathological conditions. This approach allowed us to establish a quantitative systems pharmacology framework to investigate BBB dysfunction in AD and metabolic syndrome, thereby offering opportunities to identify specific disruptions in molecular networks that will enable us to identify novel therapeutic targets.