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Welcome to The Visible Embryo, a comprehensive educational resource on human development from conception to birth.

The Visible Embryo provides visual references for changes in fetal development throughout pregnancy and can be navigated via fetal development or maternal changes.

The National Institutes of Child Health and Human Development awarded Phase I and Phase II Small Business Innovative Research Grants to develop The Visible Embryo. Initally designed to evaluate the internet as a teaching tool for first year medical students, The Visible Embryo is linked to over 600 educational institutions and is viewed by more than one million visitors each month.

Today, The Visible Embryo is linked to over 600 educational institutions and is viewed by more than 1 million visitors each month. The field of early embryology has grown to include the identification of the stem cell as not only critical to organogenesis in the embryo, but equally critical to organ function and repair in the adult human. The identification and understanding of genetic malfunction, inflammatory responses, and the progression in chronic disease, begins with a grounding in primary cellular and systemic functions manifested in the study of the early embryo.

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The World Health Organization (WHO) has created a new Web site to help researchers, doctors and
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Pregnancy Timeline by SemestersFetal liver is producing blood cellsHead may position into pelvisBrain convolutions beginFull TermWhite fat begins to be madeWhite fat begins to be madeHead may position into pelvisImmune system beginningImmune system beginningPeriod of rapid brain growthBrain convolutions beginLungs begin to produce surfactantSensory brain waves begin to activateSensory brain waves begin to activateInner Ear Bones HardenBone marrow starts making blood cellsBone marrow starts making blood cellsBrown fat surrounds lymphatic systemFetal sexual organs visibleFinger and toe prints appearFinger and toe prints appearHeartbeat can be detectedHeartbeat can be detectedBasic Brain Structure in PlaceThe Appearance of SomitesFirst Detectable Brain WavesA Four Chambered HeartBeginning Cerebral HemispheresFemale Reproductive SystemEnd of Embryonic PeriodEnd of Embryonic PeriodFirst Thin Layer of Skin AppearsThird TrimesterSecond TrimesterFirst TrimesterFertilizationDevelopmental Timeline
CLICK ON weeks 0 - 40 and follow along every 2 weeks of fetal development
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Home | Pregnancy Timeline | News Alerts |News Archive Dec 12, 2013

 

Illustration of the main driving forces behind protein structure formation.
A protein molecule folds spontaneously during or after generating a new protein.
In the compact fold (to the right), the water resistant amino acids
(shown as black spheres) are in general shielded from the water or lipid bilayer.
Folding also depends on the concentration of salts, pH balance, temperature,
the possible presence of cofactors and molecular chaperones.

Image credit: Wikipedia







WHO Child Growth Charts

 

 

 

New approach could cure wide range of diseases

Misfolded protein molecules, caused by gene mutation, are capable of maintaining their function but are misrouted within the cell and can’t work normally, thus causing disease.

Scientists have now discovered a way to use small molecules to enter cells, fix the misfolded proteins and allow them to move to the correct place and function normally again.

The researchers at Oregon Health & Science University (OHSU) were led by P. Michael Conn, Ph.D., who was a senior scientist in reproductive sciences and neuroscience at OHSU's Oregon National Primate Research Center and professor of physiology and pharmacology, cell biology and development and obstetrics and gynecology at OHSU for the past 19 years. This month, Conn joined Texas Tech University Health Sciences Center as senior vice president for research and associate provost.

The team’s work will be published this week in the early online edition of the Proceedings of the National Academy of Sciences. The work was the culmination of 13 years of work on the process by Conn and Jo Ann Janovick, former senior research associate at the ONPRC who is now also at TTUHSC. Richard R. Behringer, Ph.D., from the University of Texas MD Anderson Cancer Center, M. David Stewart, Ph.D., from the University of Houston, and Douglas Stocco, Ph.D., and Pulak Manna, Ph.D., from the department of biochemistry/microbiology at TTUHSC, also contributed to the work.

Conn and his team perfected the process in mice, curing them of a form of disease that causes males to be unable to father offspring. The identical disease occurs in humans and Conn believes the same concept can work to cure human disease as well.

"The opportunity here is going to be enormous," said Conn, "because so many human diseases are caused by misfolded proteins. The ability of these drugs – called ‘pharmacoperones’ – to rescue misfolded proteins and return them to normalcy could someday be an underlying cure to a number of diseases. Drugs that act by regulating the trafficking of molecules within cells are a whole new way of thinking about treating disease.”


Proteins must fold into three-dimensional shapes in precise ways to do their work within human cells. Before recent discoveries about misfolded proteins, scientists believed that proteins that were inactive were intrinsically non-functional.

But work by Conn and others revealed that, when the proteins are misfolded, the cell's "quality control system" misroutes them within the cell and they cease to function only because of that misrouting.

Pharmacoperones can fix misfolded proteins and thus make them functional again.

Scientists had in recent years observed this process in cells under a microscope. The work of Conn's team is the first time the process has worked in a living laboratory animal.


“These findings show how valuable laboratory animals are in identifying new treatments for human disease,” said Conn. “We expect that these studies will change the way drug companies look for drugs, since current screening procedures would have missed many useful pharmacoperone drugs.”

A wide range of diseases are caused by an accumulation of misfolded proteins. Among the diseases are neurodegenerative diseases like Alzheimer's disease, Parkinson's disease and Huntington's disease. Other diseases include certain types of diabetes, inherited cataracts and cystic fibrosis.

Conn said the next steps will be clinical trials to see whether the same technique can work in humans.

Significance
Many diseases result from genetic mutations that cause protein misfolding. Medical treatments often address the symptoms, but do not correct the underlying etiology. This study illustrates proof of principle that a disease caused by a misfolded cell surface receptor can be corrected with a pharmacoperone, a unique class of target-specific drugs that assist protein folding.

Abstract
Mutations in receptors, ion channels, and enzymes are frequently recognized by the cellular quality control system as misfolded and retained in the endoplasmic reticulum (ER) or otherwise misrouted. Retention results in loss of function at the normal site of biological activity and disease. Pharmacoperones are target-specific small molecules that diffuse into cells and serve as folding templates that enable mutant proteins to pass the criteria of the quality control system and route to their physiologic site of action. Pharmacoperones of the gonadotropin releasing hormone receptor (GnRHR) have efficacy in cell culture systems, and their cellular and biochemical mechanisms of action are known. Here, we show the efficacy of a pharmacoperone drug in a small animal model, a knock-in mouse, expressing a mutant GnRHR. This recessive mutation (GnRHR E90K) causes hypogonadotropic hypogonadism (failed puberty associated with low or apulsatile luteinizing hormone) in both humans and in the mouse model described. We find that pulsatile pharmacoperone therapy restores E90K from ER retention to the plasma membrane, concurrently with responsiveness to the endogenous natural ligand, gonadotropin releasing hormone, and an agonist that is specific for the mutant. Spermatogenesis, proteins associated with steroid transport and steroidogenesis, and androgen levels were restored in mutant male mice following pharmacoperone therapy. These results show the efficacy of pharmacoperone therapy in vivo by using physiological, molecular, genetic, endocrine and biochemical markers and optimization of pulsatile administration. We expect that this newly appreciated approach of protein rescue will benefit other disorders sharing pathologies based on misrouting of misfolded protein mutants.

The research was funded by the National Institutes of Health (grants OD012220 and DK85040), the Ben F. Love Endowment, the American Heart Association, the Texas Heart Institute and the Robert A. Welch Foundation.

About ONPRC
The ONPRC is one of the eight National Primate Research Centers supported by NIH. ONPRC is a registered research institution, inspected regularly by the United States Department of Agriculture. It operates in compliance with the Animal Welfare Act and has an assurance of regulatory compliance on file with the National Institutes of Health. The ONPRC also participates in the voluntary accreditation program overseen by the Association for Assessment and Accreditation of Laboratory Animal Care International (AAALAC).

About OHSU
Oregon Health & Science University is a nationally prominent research university and Oregon’s only public academic health center. It serves patients throughout the region with a Level 1 trauma center and nationally recognized Doernbecher Children’s Hospital. OHSU operates dental, medical, nursing and pharmacy schools that rank high both in research funding and in meeting the university’s social mission. OHSU’s Knight Cancer Institute helped pioneer personalized medicine through a discovery that identified how to shut down cells that enable cancer to grow without harming healthy ones. OHSU Brain Institute scientists are nationally recognized for discoveries that have led to a better understanding of Alzheimer’s disease and new treatments for Parkinson’s disease, multiple sclerosis and stroke. OHSU’s Casey Eye Institute is a global leader in ophthalmic imaging, and in clinical trials related to eye disease.