| 1892 |
C.H. McIlraith's paper describing families who experienced conditions of excessive thirst and frequent urination was published. This was the first reference to appear of what was probably an inherited factor in the disorder.
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| 1945 |
Renal diabetes insipidus was independently recognized as a distinct condition by Forssmann in Sweden and Waring, et al., in the U.S.A.
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| 1947 |
The term Nephrogenic Diabetes Insipidus was first used by R. H. Williams and C. Henry who determined that the symptoms of some DI patients were not alleviated by the injection of antidiuretic hormone.
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| 1954 |
The presence of the biologically active antidiuretic hormone arginine vasopressin (AVP) was found in the urine of NDI patients.
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| 1963 |
Active AVP was found in the blood of NDI patients.
|
| 1969 |
Bode and Crawford proposed under the term "The Hopewell Hypothesis" that most cases in America could be traced to descendants of Ulster Scots who arrived in Novia Scotia in 1761 on the ship Hopewell.
Nephrogenic Diabetes Insipidus in North America. The Hopewell Hypothesis
Bode, Hans H.; Crawford, M.D., John D.
New England Journal of Medicine 280:750-754, 1969.
See also, X-Linked Nephrogenic Diabetes Insipidus Mutations in North America and the Hopewell Hypothesis
Bichet, Daniel G.; Arthus, Marie-Francoise; Lonergan, Michele; Hendy, PhD, Geoffrey N.; Paradis, Ann Josee; Fujiwara, T. Mary; Morgan, Kenneth; Gregory, Martin C.; Rosenthal, Walter; Didwania, Arati
Journal of Clinical Investigation 92: 1262-1268, 1993. |
|
| 1981 |
G.L. Robertson and J.A. Scheidler provided evidence of a variant of familial NDI characterized by partial resistance to vasopressin.
A newly recognized variant of familial nephrogenic diabetes insipidus distinguished by partial resistance to vasopressin.
Gary Robertson and Scheidler, J.A.
Clinical Research 29: 555A, 1981. |
|
| 1987 |
Nine Knoers localized the gene that, when mutated, caused the most common type of inherited NDI. This was the vasopressin-2 receptor (V2R) gene.
|
| 1987 |
Mariel Birnbaumer isolated the cell line expressing the V2 receptor.
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| 1989 |
Daniel Bichet determined that NDI patients were not responding to dDAVP, a synthetic analog of AVP.
Epinephrine and dDAVP Administration in Patients with Congenital Nephrogenic Diabetes Insipidus. Evidence for a pre-cyclic AMP V2 Receptor Defective Mechanism
Bichet, Daniel G.; Razi, Mohammad; Arthus, Marie-Francoise; Lonergan, Michele; Tittley, Pauline; Smiley, Robert K.; Rock, PhD, MD, FRCP, Gail; Hirsch, David J.
Kidney International 36(5):859-66, 1989. |
|
| 1992 |
The gene and the cDNA for the V2 receptor were isolated by Mariel Birnbaumer.
Molecular Cloning of the Receptor for Human Antidiuretic Hormone
Birnbaumer, Mariel; Seibold, Anita; Gilbert, Stephanie; Ishido, Ph.D., Masami; Barberis, Claude; Antaramian, Anaid; Brabet, Philippe; Rosenthal, Walter
Nature 357(6376):333-5, 5-28-92. |
|
| 1992 |
Lolait, et al., clone a vasopressin V2 receptor of a rat and suggest its connection to nephrogenic diabetes insipidus.
|
| 1992 |
Dr. Birnbaumer's laboratory provided biochemical proof that the mutated V2R receptor is the cause of X-linked NDI.
Molecular Identification of the Gene Responsible for Congenital Nephrogenic Diabetes Insipidus
Rosenthal, Walter; Seibold, Anita; Antaramian, Anaid; Lonergan, Michele; Arthus, Marie-Francoise; Hendy, PhD, Geoffrey N.; Birnbaumer, Mariel; Bichet, Daniel G.
Nature 359(6392):233-5, 9-17-92. |
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| 1992 |
Mariel Birnbaumer, et al., deduced the primary structure of the human V2R.
|
| 1993 |
Vasopressin-regulated water channel (AQP2) cDNA was isolated by Fushimi, K., et al., in the rat.
Cloning and Expression of Apical Membrane Water Channel of Rat Kidney Collecting Tubule
Fushimi, MD, Kiyohide; Uchida, Shinichi; Hara, Yukichi; Hirata, MD, Yukio; Marumo, MD, Fumiaki; Sasaki, Sei
Nature 361(6412):549-52, 2-11-93. |
|
| 1993 |
After the isolation of the V2 receptor cDNA and gene, Dr. Birnbaumer's laboratory confirmed that the gene mapped to the same region of the X chromosome to which NDI had been previously mapped by genetic linkage analysis.
|
| 1994 |
Between 1992 and 1994, Dr. Birnbaumer's laboratory identified the first mutations in the V2 receptor gene in individuals affected with NDI that had been clinically characterized by Dr. Daniel Bichet, and confirmed biochemically that a receptor bearing those mutations did not function in vitro as the normal receptor does. This joint effort of medicine, molecular biology and biochemistry established the receptor mutations as the most common cause of NDI.
Nephrogenic Diabetes Insipidus. A V2 Vasopressin Receptor Unable to Stimulate Adenylyl Cyclase
Birnbaumer, Mariel; Rosenthal, Walter; Antaramian, Anaid; Gilbert, Stephanie
Journal of Biological Chemistry 268(18):13030-3, 6-25-93.
Mutations in the Vasopressin V2 Receptor Gene in Families with Nephrogenic Diabetes Insipidus and Functional Expression of the Q-2 Mutant
Rosenthal, Walter; Seibold, Anita; Antaramian, Anaid; Gilbert, Stephanie; Birnbaumer, Mariel; Bichet, Daniel G.; Arthus, Marie-Francoise; Lonergan, Michele
Cellular and Molecular Biology 40(3):429-36, 5-1-94. |
|
| 1994 |
The human cDNA for AQP2 was isolated and its chromosomal localization was assigned to 12q13 by Sasaki, et al.
Cloning, Characterization, and Chromosomal Mapping of Human Aquaporin of Collecting Duct
Sasaki, Sei; Fushimi, MD, Kiyohide; Saito, Hidehiko; Saito, Fumiko; Uchida, Shinichi; Ishibashi, Kenichi; Kuwahara, Michio; Ikeuchi, Tatsuro; Inui, Ken-ichi; Nakajima, Kiichird; Watanabe, Tohru; Marumo, MD, Fumiaki
Journal of Clinical Investigation 93(3):1250-6, 3-1-94
Isolation of Human aquaporin-CD Gene
Uchida, Shinichi; Sasaki, Sei; Fushimi, MD, Kiyohide; Marumo, MD, Fumiaki
Journal of Biological Chemistry 269(38):23451-5, 9-23-94. |
|
| 1994 |
The Nijmegan group of The Netherlands isolated the human cDNA for the AQP2 water channel gene and identified mutations of the AQP2 gene as a cause of the recessive form of NDI.
Patients with Autosomal Nephrogenic Diabetes Insipidus Homozygous for Mutations in the Aquaporin 2 Water-Channel Gene
van Lieburg, Angenita; Verdijk, Marian A.J.; Knoers, Nine; van Essen, A.J.; Proesmans, W.; Mallmann, Rudolf; Monnens, Leo A.H.; van Oost, Bernard A.; van Os, Carel; Deen, Peter M.T.
American Journal of Human Genetics 55(4):648-52, 10-1-94. |
Requirement of Human Renal Water Channel Aquaporin-2 for Vasopressin-Dependent Concentration of Urine
Deen, Peter M.T.; Verdijk, Marian A.J.; Knoers, Nine; Wieringa, Be; Monnens, Leo A.H.; van Os, Carel; van Oost, Bernard A.
Science 264(5155):92-5, 4-94. |
|
| 1994 |
The human AQP2 gene was mapped to the long arm of chromosome 12.
|
| 1995 |
The first demonstration of changes in AQP2 in association with NDI are documented by David Marples, et al.
|
| 1995 |
Deen, et al., provided cell biological proof that mutant AQP2 proteins, coded for by patients with recessive NDI, are impaired in their transport to the plasma membrane (export from the endoplasmic reticulum).
|
| 1998 |
Mulders, et al., provided the first evidence that autosomal dominant NDI is also caused by a mutation in the AQP2 gene and that this form of NDI is also caused by an impaired transport of the mutant AQP2 protein to the plasma membrane (retained in the Golgi Complex).
An Aquaporin-2 Water Channel Mutant Which Causes Autosomal Dominant Nephrogenic Diabetes Insipidus is Retained in the Golgi Complex
Morgan, Kenneth; Deen, Peter M.T.; Kamsteeg, Erik-Jan; Lonergan, Michele; Leijendekker, Richtje; van der Sluijs, Peter; Bichet, Daniel G.; Mulders, Sabine M.; Fujiwara, T. Mary; Arthus, Marie-Francoise; van Os, Carel; Rijss, Johan P.L.
Journal of Clinical Investigation 102(1):57-66. 7-1-98. |
|
| 1998 |
Two new mutations in the AQP2 gene causing NDI were identified by Goji, K., et al.
Novel Mutations in Aquaporin-2 Gene in Female Siblings with Nephrogenic Diabetes Insipidus: Evidence of Disrupted Water Channel Function
Goji, Katsumi; Kuwahara, Michio; Gu, Yong; Matsuo, Masafumi; Marumo, MD, Fumiaki; Sasaki, Sei
[[publisher_for_art
factor
DEFINITION:
1. Any of several substances or activities that are necessary to produce a result, e.g., a coagulation factor (see below). Often, use of the term "factor" indicates that the chemical nature of the substance or its mechanism of action is unknown, as in endocrinology, where "factors" are renamed as "hormones" when their chemical nature is determined.
2. One of two or more quantities that multiplied together form a product.
3. A gene (hereditary factor).
Antihemophilic Factor (AHF) -
1. See Factor VIII under coagulation factor (below).
2. [USP] A sterile freeze-dried powder containing the Factor VIII fraction prepared from units of human venous plasma obtained from suitable whole-blood donors; it may contain heparin sodium or sodium citrate. Used to arrest hemorrhage or to prevent hemorrhage during surgery or other procedures in patients with hemophilia A; administered intravenously.
Coagulation Factors - Substances in the blood that are essential to the clotting process and hence, to the maintenance of normal hemostasis. They are designated by Roman numerals, to which the notation "a" is added to indicate the activated state. Platelet factors (see below), designated by Arabic numerals, also play a role in coagulation.
Coagulation Factor II, prothrombin - A plasma protein that is converted to the active form thrombin (factor IIa) by cleavage by activated factor X (Xa) in the common pathway of blood coagulation; thrombin then cleaves fibrinogen to its active form fibrin. Deficiency of the factor leads to hypoprothrombinemia.
Coagulation Factor III, tissue thromboplastin - A lipoprotein functioning in the extrinsic pathway of blood coagulation, activating factor X (see below).
Coagulation Factor V, proaccelerin - A heat- and storage-labile material, present in plasma but not in serum, functioning in both the intrinsic and extrinsic pathways of blood coagulation. Deficiency of this factor, an autosomal recessive trait, leads to a rare hemorrhagic tendency, known as Owren's disease or parahemophilia, which varies greatly in severity.
Coagulation Factor VIII, antihemophilic factor (AHF) - A relatively storage-labile factor (see below) participating only in the intrinsic pathway of blood coagulation. Deficiency of this factor, when transmitted as a sex-linked recessive trait, causes classical hemophilia (hemophilia A). (See also antihemophilic factor above.)
Coagulation Factor IX, plasma thromboplastin component (PTC) - A relatively storage-stable substance involved in the intrinsic pathway of blood coagulation; upon activation, it activates factor X (see below). Deficiency results in a hemorrhagic syndrome called hemophilia B, resembling hemophilia A. Called also autoprothrombin II, Christmas factor, and antihemophilic factor B.
Coagulation Factor X, Stuart factor - A storage-stable factor that participates in both the intrinsic and extrinsic pathways of blood coagulation, uniting them to begin the common pathway of coagulation. Once activated, it forms a complex with calcium, phospholipid, and factor V (see above); the complex (prothrombinase) can cleave and activate prothrombin to thrombin. Deficiency of this factor may cause a systemic coagulation disorder.
Coagulation Factor XI, plasma thromboplastin antecedent (PTA) - A stable factor involved in the intrinsic pathway of blood coagulation; once activated, it activates factor IX. Deficiency of this factor results in a systemic blood-clotting defect called hemophilia C, which may resemble hemophilia A. Called also antihemophilic factor C.
Coagulation Factor XII, Hageman factor - A stable factor activated by contact with glass or other foreign surfaces, which initiates the intrinsic process of blood coagulation by activating factor XI and participates in activation of the kinin and fibrinolytic pathways. Deficiency of this factor results in a tendency toward thrombotic disorders, due to lack of activation of the fibrinolytic pathway. Called also glass factor, contact factor, or activation factor.
Heat-labile Factor - See Factor V under Coagulation Factors (above).
Platelet Factor - Factors important in hemostasis which are contained in or attached to the platelets.
Storage-labile Factor - A factor which shows chemically-unstable attributes during storage.
von Willebrand Factor (vWF) - The attribute of factor VIII (see above) necessary for the adhesion of platelets to vascular elements. Deficiency of this factor results in the prolonged bleeding time seen in von Willebrand's disease.
proteins
DEFINITION:
Any of a group of complex organic compounds which contain carbon, hydrogen, oxygen, nitrogen, and usually sulfur, the characteristic element being nitrogen, and which are widely distributed in plants and animals. Proteins, the principal constituents of the protoplasm of all cells, are of high molecular weight and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and each protein has a unique, genetically defined amino acid sequence which determines its specific shape and function. They serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved in oxygen transport, muscle contraction, electron transport, and other activities throughout the body, and in photosynthesis.
binding protein - any of a number of plasma proteins (See below) that bind to hormones of low solubility (chiefly the thyroid and steroid hormones), thus providing a transport system for them; some are specific for particular hormones, while others bind to any sparingly soluble hormones. Called also carrier protein or transport protein (See below).
carrier proteins - A binding protein (See above).
plasma proteins - The hundreds of different proteins present in blood plasma, including carrier proteins (such as albumin, transferrin, and haptoglobin), fibrinogen and other coagulation factors, complement components, immunoglobulins, enzyme inhibitors, precursors of substances such as angiotensin and bradykinin, and many other types of proteins.
transport protein - binding protein (See above).
protein
DEFINITION:
Any of a group of complex organic compounds which contain carbon, hydrogen, oxygen, nitrogen, and usually sulfur, the characteristic element being nitrogen, and which are widely distributed in plants and animals. Proteins, the principal constituents of the protoplasm of all cells, are of high molecular weight and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and each protein has a unique, genetically defined amino acid sequence which determines its specific shape and function. They serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved in oxygen transport, muscle contraction, electron transport, and other activities throughout the body, and in photosynthesis.
binding protein - any of a number of plasma proteins (See below) that bind to hormones of low solubility (chiefly the thyroid and steroid hormones), thus providing a transport system for them; some are specific for particular hormones, while others bind to any sparingly soluble hormones. Called also carrier protein or transport protein (See below).
carrier proteins - A binding protein (See above).
plasma proteins - The hundreds of different proteins present in blood plasma, including carrier proteins (such as albumin, transferrin, and haptoglobin), fibrinogen and other coagulation factors, complement components, immunoglobulins, enzyme inhibitors, precursors of substances such as angiotensin and bradykinin, and many other types of proteins.
transport protein - binding protein (See above).
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