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Renin
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For the places in Iran, see Renin, Iran.
Not to be confused with rennin, the active enzyme in rennet.
REN
Available structures
PDB
Ortholog search: PDBe RCSB
showList of PDB id codes
4XX4, 1BBS, 1BIL, 1BIM, 1HRN, 1RNE, 2BKS, 2BKT, 2FS4, 2G1N, 2G1O, 2G1R, 2G1S, 2G1Y, 2G20, 2G21, 2G22, 2G24, 2G26, 2G27, 2I4Q, 2IKO, 2IKU, 2IL2, 2REN, 2V0Z, 2V10, 2V11, 2V12, 2V13, 2V16, 2X0B, 3D91, 3G6Z, 3G70, 3G72, 3GW5, 3K1W, 3KM4, 3O9L, 3OAD, 3OAG, 3OOT, 3OQF, 3OQK, 3OWN, 3Q3T, 3Q4B, 3Q5H, 3SFC, 3VCM, 3VSW, 3VSX, 3VUC, 3VYD, 3VYE, 3VYF, 4AMT, 4GJ5, 4GJ6, 4GJ7, 4GJ8, 4GJ9, 4GJA, 4GJB, 4GJC, 4GJD, 4PYV, 4Q1N, 4RYC, 4RYG, 4RZ1, 4S1G, 4XX3
Identifiers
Aliases
REN, HNFJ2, renin
External IDs
OMIM: 179820 MGI: 97898 HomoloGene: 20151 GeneCards: REN
hideGene location (Human)
Chr.
Chromosome 1 (human)[1]
Band
1q32.1
Start
204,154,819 bp[1]
End
204,190,324 bp[1]
showGene location (Mouse)
Chr.
Chromosome 1 (mouse)[2]
Band
1 E4|1 57.91 cM
Start
133,350,510 bp[2]
End
133,360,325 bp[2]
showGene ontology
Molecular function
• insulin-like growth factor receptor binding
• aspartic-type endopeptidase activity
• endopeptidase activity
• peptidase activity
• receptor binding
• hydrolase activity
• protein binding
Cellular component
• cytoplasm
• membrane
• plasma membrane
• intracellular
• extracellular region
• extracellular space
• apical part of cell
Biological process
• response to immobilization stress
• regulation of blood volume by renin-angiotensin
• male gonad development
• regulation of MAPK cascade
• kidney development
• renin-angiotensin regulation of aldosterone production
• cell maturation
• amyloid-beta metabolic process
• response to organic substance
• angiotensin maturation
• proteolysis
• mesonephros development
• regulation of blood pressure
• response to lipopolysaccharide
• cellular response to drug
• protein catabolic process
• drinking behavior
• hormone-mediated signaling pathway
• response to cGMP
• response to cAMP
• response to drug
Sources:Amigo / QuickGO
Orthologs
Species
Human Mouse
Entrez
5972
19701
Ensembl
ENSG00000143839
ENSMUSG00000070645
UniProt
P00797
P06281
RefSeq (mRNA)
NM_000537
NM_031192
RefSeq (protein)
NP_000528
NP_112469
Location (UCSC)
Chr 1: 204.15 – 204.19 Mb Chr 1: 133.35 – 133.36 Mb
PubMed search
[3] [4]
Wikidata
View/Edit Human View/Edit Mouse
renin
Identifiers
EC number
3.4.23.15
CAS number
9015-94-5
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
showSearch
PMC
articles
PubMed
articles
NCBI
proteins
Renin (etymology and pronunciation), also known as an angiotensinogenase, is an aspartic protease protein and enzyme secreted by the kidneys that participates in the body's renin–angiotensin–aldosterone system (RAAS)—also known as the renin–angiotensin–aldosterone axis—that mediates the volume of extracellular fluid (blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. Thus, it regulates the body's mean arterial blood pressure.
Renin can be referred to as a hormone even though it has no peripheral receptors and rather has an enzymatic activity with which it hydrolyzes angiotensinogen to angiotensin I.
Contents
1 Biochemistry and physiology
1.1 Structure
1.2 Secretion
1.3 Renin–angiotensin system
2 Function
3 Genetics
3.1 Model organisms
4 Clinical applications
4.1 Measurement
5 Discovery and naming
6 See also
7 References
8 External links
Biochemistry and physiology[edit]
Structure[edit]
The primary structure of renin precursor consists of 406 amino acids with a pre- and a pro-segment carrying 20 and 46 amino acids, respectively. Mature renin contains 340 amino acids and has a mass of 37 kDa.[5]
Secretion[edit]
The enzyme renin is secreted by pericytes (mural cells) (1) in vicinity of the afferent arterioles and similar microvessels of the kidney from specialized cells of the juxtaglomerular apparatus—the juxtaglomerular cells, in response to three stimuli:
A decrease in arterial blood pressure (that could be related to a decrease in blood volume) as detected by baroreceptors (pressure-sensitive cells). This is the most direct causal link between blood pressure and renin secretion (the other two methods operate via longer pathways).
A decrease in sodium load delivered to the distal tubule. This load is measured by the macula densa of the juxtaglomerular apparatus.
Sympathetic nervous system activity, which also controls blood pressure, acting through the β1 adrenergic receptors.
Human renin is secreted by at least 2 cellular pathways: a constitutive pathway for the secretion of the precursor prorenin and a regulated pathway for the secretion of mature renin.[6]
Renin–angiotensin system[edit]
Main article: Renin–angiotensin system
The renin–angiotensin system, showing role of renin at bottom.[7]
The renin enzyme circulates in the blood stream and hydrolyzes (breaks down) angiotensinogen secreted from the liver into the peptide angiotensin I.
Angiotensin I is further cleaved in the lungs by endothelial-bound angiotensin-converting enzyme (ACE) into angiotensin II, the most vasoactive peptide.[8][9] Angiotensin II is a potent constrictor of all blood vessels. It acts on the smooth muscle and, therefore, raises the resistance posed by these arteries to the heart. The heart, trying to overcome this increase in its 'load', works more vigorously, causing the blood pressure to rise. Angiotensin II also acts on the adrenal glands and releases aldosterone, which stimulates the epithelial cells in the distal tubule and collecting ducts of the kidneys to increase re-absorption of sodium, exchanging with potassium to maintain electrochemical neutrality, and water, leading to raised blood volume and raised blood pressure. The RAS also acts on the CNS to increase water intake by stimulating thirst, as well as conserving blood volume, by reducing urinary loss through the secretion of vasopressin from the posterior pituitary gland.
The normal concentration of renin in adult human plasma is 1.98–24.6 ng/L in the upright position.[10]
Function[edit]
Renin activates the renin–angiotensin system by cleaving angiotensinogen, produced by the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE, the angiotensin–converting enzyme primarily within the capillaries of the lungs. Angiotensin II then constricts blood vessels, increases the secretion of ADH and aldosterone, and stimulates the hypothalamus to activate the thirst reflex, each leading to an increase in blood pressure. Renin's primary function is therefore to eventually cause an increase in blood pressure, leading to restoration of perfusion pressure in the kidneys.
Renin is secreted from juxtaglomerular kidney cells, which sense changes in renal perfusion pressure, via stretch receptors in the vascular walls. The juxtaglomerular cells are also stimulated to release renin by signaling from the macula densa. The macula densa senses changes in sodium delivery to the distal tubule, and responds to a drop in tubular sodium load by stimulating renin release in the juxtaglomerular cells. Together, the macula densa and juxtaglomerular cells comprise the juxtaglomerular complex.
Renin secretion is also stimulated by sympathetic nervous stimulation, mainly through beta-2 adrenergic receptor (β1 adrenoreceptor) activation.
Renin can bind to ATP6AP2, which results in a fourfold increase in the conversion of angiotensinogen to angiotensin I over that shown by soluble renin. In addition, renin binding results in phosphorylation of serine and tyrosine residues of ATP6AP2.[11]
The level of renin mRNA appears to be modulated by the binding of HADHB, HuR and CP1 to a regulatory region in the 3' UTR.[12]
Genetics[edit]
The gene for renin, REN, spans 12 kb of DNA and contains 8 introns.[13] It produces several mRNA that encode different REN isoforms.
Mutations in the REN gene can be inherited, and are a cause of a rare inherited kidney disease, so far found to be present in only 2 families. This disease is autosomal dominant, meaning that it is characterized by a 50% chance of inheritance and is a slowly progressive chronic kidney disease that leads to the need for dialysis or kidney transplantation. Many—but not all—patients and families with this disease suffer from an elevation in serum potassium and unexplained anemia relatively early in life. Patients with a mutation in this gene can have a variable rate of loss of kidney function, with some individuals going on dialysis in their 40s while others may not go on dialysis until into their 70s. This is a rare inherited kidney disease that exists in less than 1% of people with kidney disease.[14]
Model organisms[edit]
Ren1 knockout mouse phenotype show
Characteristic
Phenotype
Homozygote viability Normal
Fertility Normal
Body weight Normal
Anxiety Normal
Neurological assessment Normal
Grip strength Normal
Hot plate Normal
Dysmorphology Normal
Non-Invasive Blood Pressure Abnormal[15]
Indirect calorimetry Normal
Glucose tolerance test Normal
Auditory brainstem response Normal
DEXA Normal
Radiography Normal
Body temperature Normal
Eye morphology Normal
Clinical chemistry Normal
Haematology Normal
Micronucleus test Normal
Heart weight Normal
Skin Histopathology Normal
Brain histopathology Normal
Salmonella infection Normal[16]
Citrobacter infection Abnormal[17]
All tests and analysis from[18][19]
Model organisms have been used in the study of REN function. A knockout mouse line, called Ren1Ren-1c Enhancer KO was generated.[20] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[18][21] Twenty four tests were carried out on mutant mice and two significant abnormalities were observed. Homozygous mutant animals had a decreased heart rate and an increased susceptibility to bacterial infection.[18] A more detailed analysis of this line indicated plasma creatinine was also increased and males had lower mean arterial pressure than controls.[20]
Clinical applications[edit]
Main article: Renin inhibitor
An over-active renin-angiotension system leads to vasoconstriction and retention of sodium and water. These effects lead to hypertension. Therefore, renin inhibitors can be used for the treatment of hypertension.[22][23] This is measured by the plasma renin activity (PRA).
In current medical practice, the renin–angiotensin–aldosterone system's overactivity (and resultant hypertension) is more commonly reduced using either ACE inhibitors (such as ramipril and perindopril) or angiotensin II receptor blockers (ARBs, such as losartan, irbesartan or candesartan) rather than a direct oral renin inhibitor. ACE inhibitors or ARBs are also part of the standard treatment after a heart attack.
The differential diagnosis of kidney cancer in a young patient with hypertension includes juxtaglomerular cell tumor (reninoma), Wilms' tumor, and renal cell carcinoma, all of which may produce renin.[24]
Measurement[edit]
Further information: Plasma renin activity
Renin is usually measured as the plasma renin activity (PRA). PRA is measured specially in case of certain diseases that present with hypertension or hypotension. PRA is also raised in certain tumors.[25] A PRA measurement may be compared to a plasma aldosterone concentration (PAC) as a PAC/PRA ratio.
Discovery and naming[edit]
The name renin = ren + -in, "kidney" + "compound". The most common pronunciation in English is /ˈriːnɪn/ (long e); /ˈrɛnɪn/ (short e) is also common, but using /ˈriːnɪn/ allows one to reserve /ˈrɛnɪn/ for rennin. Renin was discovered, characterized, and named in 1898 by Robert Tigerstedt, Professor of Physiology, and his student, Per Bergman, at the Karolinska Institute in Stockholm.[26][27]
See also[edit]
Angiotensin-converting enzyme
Plasma renin activity
Renin inhibitor
Renin stability regulatory element (REN-SRE)
References[edit]
^ Jump up to: a b c GRCh38: Ensembl release 89: ENSG00000143839 - Ensembl, May 2017
^ Jump up to: a b c GRCm38: Ensembl release 89: ENSMUSG00000070645 - Ensembl, May 2017
Jump up ^ "Human PubMed Reference:".
Jump up ^ "Mouse PubMed Reference:".
Jump up ^ Imai T, Miyazaki H, Hirose S, Hori H, Hayashi T, Kageyama R, Ohkubo H, Nakanishi S, Murakami K (Dec 1983). "Cloning and sequence analysis of cDNA for human renin precursor". Proceedings of the National Academy of Sciences of the United States of America. 80 (24): 7405–9. doi:10.1073/pnas.80.24.7405. PMC 389959  . PMID 6324167.
Jump up ^ Pratt RE, Flynn JA, Hobart PM, Paul M, Dzau VJ (Mar 1988). "Different secretory pathways of renin from mouse cells transfected with the human renin gene". The Journal of Biological Chemistry. 263 (7): 3137–41. PMID 2893797.
Jump up ^ Boulpaep EL, Boron WF (2005). "Integration of Salt and Water Balance; The Adrenal Gland". Medical physiology: a cellular and molecular approach. St. Louis, MO: Elsevier Saunders. pp. 866–867, 1059. ISBN 1-4160-2328-3.
Jump up ^ Fujino T, Nakagawa N, Yuhki K, Hara A, Yamada T, Takayama K, Kuriyama S, Hosoki Y, Takahata O, Taniguchi T, Fukuzawa J, Hasebe N, Kikuchi K, Narumiya S, Ushikubi F (Sep 2004). "Decreased susceptibility to renovascular hypertension in mice lacking the prostaglandin I2 receptor IP". The Journal of Clinical Investigation. 114 (6): 805–12. doi:10.1172/JCI21382. PMC 516260  . PMID 15372104.
Jump up ^ Brenner & Rector's The Kidney, 7th ed., Saunders, 2004, pp. 2118-2119 Full Text with MDConsult subscription
Jump up ^ Hamilton Regional Laboratory Medicine Program - Laboratory Reference Centre Manual. [deadlink]
Jump up ^ Nguyen G, Delarue F, Burcklé C, Bouzhir L, Giller T, Sraer JD (Jun 2002). "Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin". The Journal of Clinical Investigation. 109 (11): 1417–27. doi:10.1172/JCI14276. PMC 150992  . PMID 12045255.
Jump up ^ Adams DJ, Beveridge DJ, van der Weyden L, Mangs H, Leedman PJ, Morris BJ (Nov 2003). "HADHB, HuR, and CP1 bind to the distal 3'-untranslated region of human renin mRNA and differentially modulate renin expression". The Journal of Biological Chemistry. 278 (45): 44894–903. doi:10.1074/jbc.M307782200. PMID 12933794.
Jump up ^ Hobart PM, Fogliano M, O'Connor BA, Schaefer IM, Chirgwin JM (Aug 1984). "Human renin gene: structure and sequence analysis". Proceedings of the National Academy of Sciences of the United States of America. 81 (16): 5026–30. doi:10.1073/pnas.81.16.5026. PMC 391630  . PMID 6089171.
Jump up ^ Zivná M, Hůlková H, Matignon M, Hodanová K, Vylet'al P, Kalbácová M, Baresová V, Sikora J, Blazková H, Zivný J, Ivánek R, Stránecký V, Sovová J, Claes K, Lerut E, Fryns JP, Hart PS, Hart TC, Adams JN, Pawtowski A, Clemessy M, Gasc JM, Gübler MC, Antignac C, Elleder M, Kapp K, Grimbert P, Bleyer AJ, Kmoch S (2009). "Dominant renin gene mutations associated with early-onset hyperuricemia, anemia, and chronic kidney failure". Am. J. Hum. Genet. 85 (2): 204–13. doi:10.1016/j.ajhg.2009.07.010. PMC 2725269  . PMID 19664745.
Jump up ^ "Non-Invasive Blood Pressure data for Ren1". Wellcome Trust Sanger Institute.
Jump up ^ "Salmonella infection data for Ren1". Wellcome Trust Sanger Institute.
Jump up ^ "Citrobacter infection data for Ren1". Wellcome Trust Sanger Institute.
^ Jump up to: a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
Jump up ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
^ Jump up to: a b Adams DJ, Head GA, Markus MA, Lovicu FJ, van der Weyden L, Köntgen F, Arends MJ, Thiru S, Mayorov DN, Morris BJ (Oct 2006). "Renin enhancer is critical for control of renin gene expression and cardiovascular function". The Journal of Biological Chemistry. 281 (42): 31753–61. doi:10.1074/jbc.M605720200. PMID 16895910.
Jump up ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837  . PMID 21722353.
Jump up ^ Presentation on Direct Renin Inhibitors as Antihypertensive Drugs Archived 2010-12-07 at the Wayback Machine.
Jump up ^ Ram CV (Sep 2009). "Direct inhibition of renin: a physiological approach to treat hypertension and cardiovascular disease". Future Cardiology. 5 (5): 453–65. doi:10.2217/fca.09.31. PMID 19715410.
Jump up ^ Méndez GP, Klock C, Nosé V (Feb 2011). "Juxtaglomerular cell tumor of the kidney: case report and differential diagnosis with emphasis on pathologic and cytopathologic features". International Journal of Surgical Pathology. 19 (1): 93–8. doi:10.1177/1066896908329413. PMID 19098017.
Jump up ^ Hamilton Regional Laboratory Medicine Program - Laboratory Reference Centre Manual. Renin Direct.
Jump up ^ Phillips MI, Schmidt-Ott KM (Dec 1999). "The Discovery of Renin 100 Years Ago". News in Physiological Sciences. 14: 271–274. PMID 11390864.
Jump up ^ Tigerstedt R, Bergman PG (1898). "Niere und Kreislauf" [Kidney and Circulation]. Skandinavisches Archiv für Physiologie [Scandinavian Archives of Physiology] (in German). 8: 223–271. doi:10.1111/j.1748-1716.1898.tb00272.x.
(1) Human kidney pericytes produce renin ; Stefanska A, Kenyon C, Christian HC, Buckley C, Shaw I, Mullins JJ, Péault B. Kidney Int. 2016 Dec; 90(6):1251-1261
External links[edit]
GeneReviews/NCBI/NIH/UW entry on Familial Juvenile Hyperuricemic Nephropathy Type 2
OMIM entries on Familial Juvenile Hyperuricemic Nephropathy Type 2
The MEROPS online database for peptidases and their inhibitors: A01.007
Renin at the US National Library of Medicine Medical Subject Headings (MeSH)

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PDB gallery
2bks: CRYSTAL STRUCTURE OF RENIN-PF00074777 COMPLEX
2g24: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
2ren: STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION
2iko: Crystal Structure of Human Renin Complexed with Inhibitor
2g1y: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
2g20: Ketopiperazine-Based Renin Inhibitors: Optimization of the C Ring
2g26: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
2g1n: Ketopiperazine-based renin inhibitors: Optimization of the ""C"" ring
1bil: CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS
2iku: Crystal Structure of Human Renin Complexed with Inhibitors
2g1o: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
2g1r: Ketopiperazine-Based Renin Inhibitors: Optimization of the C Ring
1bim: CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS
2fs4: Ketopiperazine-Based Renin Inhibitors: Optimization of the C ring
2il2: Crystal Structure of Human Renin Complexed with Inhibitor
1hrn: HIGH RESOLUTION CRYSTAL STRUCTURES OF RECOMBINANT HUMAN RENIN IN COMPLEX WITH POLYHYDROXYMONOAMIDE INHIBITORS
2bkt: CRYSTAL STRUCTURE OF RENIN-PF00257567 COMPLEX
2g27: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
1rne: THE CRYSTAL STRUCTURE OF RECOMBINANT GLYCOSYLATED HUMAN RENIN ALONE AND IN COMPLEX WITH A TRANSITION STATE ANALOG INHIBITOR
2g21: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
1bbs: X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS
2g1s: Ketopiperazine-Based Renin Inhibitors: Optimization of the C Ring
2i4q: Human renin/PF02342674 complex
2g22: Ketopiperazine-Based Renin Inhibitors: Optimization of the ""C"" Ring
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Retrieved from "https://en.wikipedia.org/w/index.php?title=Renin&oldid=852171611"
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text:
List of Indian cities on rivers
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This article is an orphan, as no other articles link to it. Please introduce links to this page from related articles; try the Find link tool for suggestions. (June 2014)
The following is a list of cities in India through which gangs flows by and how:
City
River
State
Agra Yamuna Western Uttar Pradesh
Ahmedabad Sabarmati Gujarat
Allahabad At the confluence of Ganga, Yamuna and Saraswati Uttar Pradesh
Ayodhya Saryu Uttar Pradesh
Badrinath Alaknanda Uttarakhand
Banki Mahanadi Odisha
Brahmapur Rushikulya Odisha
Chhatrapur Rushikulya Odisha
Bhagalpur Ganges Bihar
Kolkata Hooghly West Bengal
Cuttack Mahanadi Odisha
New Delhi Yamuna Delhi
Dibrugarh Brahmaputra Assam
Ferozpur Sutlej Punjab
Guwahati Brahmaputra Assam
Haridwar Ganges Uttarakhand
Hyderabad Musi Telangana
Jabalpur Narmada Madhya Pradesh
Kanpur Ganges Uttar Pradesh
Kota Chambal Rajasthan
Kottayam Meenachil Kerala
Jaunpur Gomti Uttar Pradesh
Patna Ganges Bihar
Rajahmundry Godavari Andhra Pradesh
Srinagar Jhelum Jammu & Kashmir
Surat Tapi Gujarat
Varanasi Ganges Uttar Pradesh
Vijayawada Krishna Andhra Pradesh
Vadodara Vishwamitri, Mahi, Narmada Gujarat
Mathura Yamuna Uttar Pradesh
Mirzapur Ganga Uttar Pradesh
Auraiya Yamuna Uttar Pradesh
Etawah Yamuna Uttar Pradesh
Bangalore Vrishabhavathi Karnataka
Farrukhabad Ganges Uttar Pradesh
Rangpo Teesta Sikkim
Gaya Falgu (Neeranjana) Bihar
Fatehgarh Ganges Uttar Pradesh
Kannauj Ganges Uttar Pradesh
Mangalore Netravati, Gurupura Karnataka
Shimoga Tunga River Karnataka
Bhadravathi Bhadra Karnataka
Hospet Tungabhadra Karnataka
Karwar Kali Karnataka
Bagalkot Ghataprabha Karnataka
Honnavar Sharavathi Karnataka
Gwalior Chambal Madhya Pradesh
Gorakhpur Rapti Uttar Pradesh
Lucknow Gomti Uttar Pradesh
Kanpur Cantonment Ganges Uttar Pradesh
Shuklaganj Ganges Uttar Pradesh
Chakeri Ganges Uttar Pradesh
Malegaon Girna River Maharashtra
Sambalpur Mahanadi Odisha
Rourkela Brahmani Odisha
Pune Mula, Mutha Maharashtra
Daman Daman Ganga River Daman
Madurai Vaigai Tamil Nadu
Thiruchirapalli Kaveri Tamil Nadu
Chennai Cooum, Adyar Tamil Nadu
Coimbatore Noyyal Tamil Nadu
Erode Kaveri Tamil Nadu
Tirunelveli Thamirabarani Tamil Nadu
Bharuch Narmada Gujarat
Karjat Ulhas Maharashtra
Nashik Godavari Maharashtra
Mahad Savitri Maharashtra
Nanded Godavari Maharashtra
Kolhapur Panchaganga Maharashtra
Nellore Pennar Andhra Pradesh
kurnool Tungabhadra River Andhra Pradesh
Nizamabad Godavari Telangana
Sangli Krishna Maharashtra
Karad Krishna, Koyna Maharashtra
Hajipur Ganges Bihar
Ujjain Shipra Madhya Pradesh[1]
Ashta Parwati Madhya Pradesh[2]
Rishikesh Ganges Uttarakhand
[3]morhar
References[edit]
Jump up ^ Shipra River
Jump up ^ Shipra River
Jump up ^ turkaul
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